DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claim Interpretation
BRI of the claim term “nonameric peptide represented by an amino acid sequence of SEQ ID NO: 1” includes 1) the peptide consisting of RRWIALWLR (SEQ ID NO: 1), and 2) all peptides nine amino acids in length comprising a fragment of RRWIALWLR (SEQ ID NO: 1) (e.g. RR, RRW, RRWI, RRWIA etc). The claim limitation is given this interpretation because of the indefinite article “an” prior to “amino acid sequence of”. If Applicant wants to limit the scope of the claims to peptides that are nine amino acid in length consisting of full-length SEQ ID NO: 1, the indefinite article “an” should be replaced with the definite article “the”.
BRI of the claim term “enantiomeric peptide thereof” is the definition on page 14, lines 20-22: the enantiomeric peptide is characterized in that all of the amino acids of the amino acid sequence of SEQ ID NO: 1 are substituted with D-type amino acids.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1-2 and 4-13 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon without significantly more.
Claim Interpretation: BRI of claim 1 includes nonameric peptides comprising fragments of instant SEQ ID NO: 1 (see claim interpretation above). Therefore, the peptide QGGICVCRR is within the BRI of claim 1 because it is nine amino acid residues in length and comprises the dipeptide RR, which is a fragment of instant SEQ ID NO: 1.
Step 1: Claim 1 is to a composition of matter.
Step 2A, Prong 1: Claim 1 is directed to a product of nature, the peptide QGGICVCRR. The closest counterpart to the nature-based product is protaetiamycine, a defensin-like peptide from the larvae of a beetle Protaetia brevitaris. The claimed peptide corresponds to residues 70 of 79 of protaetiamycine, as evidenced by Figure 1 of Hwang1. The claimed peptide has a different structural characteristic than the natural peptide, i.e., the natural peptide has covalent bonds on its ends that connect it to the rest of the protein whereas the claimed peptide lacks these bonds. However, the claimed peptide is otherwise structurally identical to the natural peptide, e.g., it has the same peptide backbone and amino acid sequence as residues 70 of 79 of protaetiamycine in nature. This difference is not a marked difference in view of MPEP § 2106.04(c)(II)(C)(2) and the Supreme Court decision in Myriad. See, e.g., Myriad, 569 U.S. at 585, 106 USPQ2d at 1977. In addition, the function of the claimed peptide is innate to the peptide itself, and was not created or altered by the inventor. See Ambry Genetics, 774 F.3d at 760-61, 113 USPQ2d at 1244. In sum, the claimed peptide is different, but not markedly different, from its naturally occurring counterparts (residues 70 of 79 of protaetiamycine), and thus is a natural phenomenon exceptions
Step 2A, Prong 2: The claim only recites the peptide, which is a natural phenomenon exception. Because there are no additional claim elements besides the judicial exception, the judicial exception is not integrated into a practical application (MPEP § 2106.04(d)(III)).
Step 2B: The claim only recites the peptide, which is a natural phenomenon exception. Because there are no additional claim elements besides the judicial exception, the claim does not amount to significantly more than the judicial exception (MPEP § 2106.05).
Therefore, claim 1 is patent ineligible.
Claims 2 and 4-13 depend from claim 1 and encompass the same natural phenomenon exception.
Step 2A, Prong 2: The claims only recite the peptide, which is a natural phenomenon exception.
Because the additional functional limitations of claims 2 and 4-13 do not actually provide a treatment or prophylaxis, e.g., they are merely an intended use of the claimed invention or a field of use limitation, then they cannot integrate a judicial exception under the "treatment or prophylaxis" consideration (MPEP § 2106.04(d)(2)).
Step 2B: Because the additional functional limitations of claims 2 and 4-13 do not actually provide a treatment or prophylaxis, e.g., they are merely an intended use of the claimed invention or a field of use limitation, the claims do not amount to significantly more than the judicial exception (MPEP § 2106.05).
Therefore, claims 2 and 4-13 are patent ineligible.
This rejection could be overcome by amending claim 1 to “A peptide consisting of the amino acid sequence of SEQ ID NO: 1 and the enantiomeric peptide thereof.”
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 2 and 4-13 and 26 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. Only the peptides RRWIALWLR-NH2 (SEQ ID NO: 1, R-Pro9-3) and its all-D enantiomer (R-Pro9-3D) satisfy the written description provision.
In claims 1-2, 4-13, and 26, the peptides include: 1) the peptide consisting of RRWIALWLR (SEQ ID NO: 1), 2) all peptides nine amino acids in length comprising a fragment of RRWIALWLR (SEQ ID NO: 1) (e.g. RR, RRW, RRWI, RRWIA etc); and enantiomeric peptides of 1) and 2) wherein all of the amino acids are in the D-configuration. Claim 3 is limited to the peptide consisting of rrwialwlr, which is the all D-enantiomer of SEQ ID NO: 1. See claim interpretation section above.
Claims 1 and 3 are not limited by function. Claims 2, 4-13, and 26 recite functional limitations.
Only those sequences meeting the structural and functional requirements of the genus are encompassed by the claim. Although with the aid of a computer it may be possible to determine the amino acid sequences of the peptides that meet the structural requirements of the claims, it is not readily apparent from the claims or the specification which of these sequences also possess claimed functions.
Only the peptides RRWIALWLR-NH2 (SEQ ID NO: 1, R-Pro9-3) and its all-D enantiomer (R-Pro9-3D) were reduced to practice in the specification and were shown to have antimicrobial activity against Gram-negative bacteria (Example 2-4), biofilm inhibition activity (Example 5), resistance to proteases (Example 6), low cytotoxicity (Example 8), anti-inflammatory activity (Example 9), and anti-septic activity in an animal model of septic shock (Example 10).
As discussed above the claim scope is potentially enormous depending on how many of the sequences that meet the structural requirements also have antimicrobial or other claimed activity. In comparison, the scope of the description which only includes full-length SEQ ID NO: 1 and its enantiomer, is extremely narrow. The actual reduction to practice does not include species characterized by fragments of SEQ ID NO: 1. Therefore, one of ordinary skill in the art would not consider R-Pro9-3 and R-Pro9-3D to be representative of the full scope of the claimed genus.
The specification does not describe a general correlation between structure and function for the claimed genus. The role of the nine amino acids of SEQ ID NO: 1 in antimicrobial activity, LPS binding, anti-inflammatory activity, biofilm inhibition, hemolytic activity, and cytotoxicity are not described. As a result, it is impossible to predict, based on the specification, how fragmenting SEQ ID NO: 1 and embedding the fragments in nonameric sequences will affect the claimed functions.
For these reasons, the skilled artisan would not reasonably conclude that the inventor(s), at the time the application was filed, had possession of the full scope of the claimed invention.
This rejection could be overcome by amending claim 1 to “A peptide consisting of the amino acid sequence of SEQ ID NO: 1 and the enantiomeric peptide thereof.”
Claims 1-2, 4-13 and 26 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for using the peptides RRWIALWLR-NH2 (SEQ ID NO: 1, R-Pro9-3) and its all-D enantiomer (R-Pro9-3D) to treat or prevent gram-negative bacterial infection, does not reasonably provide enablement for the use of nonameric peptides comprising fragments of RRWIALWLR-NH2 and enantiomers thereof. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
To comply with the enablement requirements of 35 U.S.C. §112, first paragraph, a specification must adequately teach how to make and how to use a claimed invention throughout its scope, without undue experimentation. Plant Genetic Systems N.V. v. DeKalb Genetics Corp., 315 F.3d 1335, 1339, 65 USPQ2d 1452, 1455 (Fed. Cir. 2003). There are a variety of factors which may be considered in determining whether a disclosure would require undue experimentation. These factors include: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims. In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988).
The Nature of the Invention
The invention is in the technical field of antimicrobial peptides.
The breadth of the claims
Structure: In claims 1-2, 4-13, and 26, the peptides include: 1) the peptide consisting of RRWIALWLR (SEQ ID NO: 1), 2) all peptides nine amino acids in length comprising a fragment of RRWIALWLR (SEQ ID NO: 1) (e.g. RR, RRW, RRWI, RRWIA etc); and enantiomeric peptides of 1) and 2) wherein all of the amino acids are in the D-configuration. Claim 3 is limited to the peptide consisting of rrwialwlr, which is the all D-enantiomer of SEQ ID NO: 1.
Function: Claims 1 and 3 are not limited by function. Claims 2, 4-13, and 26 recite functional limitations.
The scope of claims 2, 4-13, and 26 is limited to peptides meeting the structural requirements of the claims that also have the claimed function.
The State of the Prior Art/ Predictability or Unpredictability of the Art
The prior art pertaining to peptide structure and function is highly unpredictable. The prior art is replete with examples of peptides wherein the change of a single amino acid has significant effect on function as well as with examples of changes with only minimal or no effect on function.
The Level of Guidance in the Specification
The specification does not describe a general correlation between structure and function for the claimed genus. The role of the nine amino acids of SEQ ID NO: 1 in antimicrobial activity, LPS binding, anti-inflammatory activity, biofilm inhibition, hemolytic activity, and cytotoxicity are not described. As a result, it is impossible to predict, based on the specification, how fragmenting SEQ ID NO: 1 and embedding the fragments in nonameric sequences will affect the claimed functions.
The Presence or Absence of Working Examples
Only the peptides RRWIALWLR-NH2 (SEQ ID NO: 1, R-Pro9-3) and its all-D enantiomer (R-Pro9-3D) were reduced to practice in the specification and were shown to have antimicrobial activity against Gram-negative bacteria (Example 2-4), biofilm inhibition activity (Example 5), resistance to proteases (Example 6), low cytotoxicity (Example 8), anti-inflammatory activity (Example 9), and anti-septic activity in an animal model of septic shock (Example 10).
The Quantity of Experimentation Necessary
Considering the factors above, the skilled artisan would be burdened with undue experimentation in determining if fragments of SEQ ID NO: 1 embedded in nonameric sequences and enantiomers thereof would be effective as antimicrobial peptides. The skilled artisan would be burdened with testing a broad range of peptides in in vitro assays. The active peptides would then have to be subjected to animal models of microbial infection. The experimentation required represents years of inventive effort. When the above factors are weighed, it is the examiner's position that one skilled in the art could not practice the invention without undue experimentation.
Therefore, in view of the Wands factors, the claims appear to require undue experimentation to use the full scope of the claimed invention.
This rejection could be overcome by amending claim 1 to “A peptide consisting of the amino acid sequence of SEQ ID NO: 1 and the enantiomeric peptide thereof.”
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1-2, 4-13 and 23 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lee (Enantiomeric 9-mer peptide analogs of protaetiamycine with bacterial cell selectivities and anti-inflammatory activities. Pept. Sci. 2011; 17: 675–682).
Claim Interpretation: BRI of claim 1 includes nonameric peptides comprising fragments of instant SEQ ID NO: 1 and its enantiomers (see claim interpretation above).
Claim Rejection: Lee teaches the peptides (Table 1):
9Pbw2 RLWLAIKRR-NH2
9Pbw3 RLWLAIWRR-NH2
9Pbw4 RLWLAWKRR-NH2
Pbw3-D RLWLAIWRR-NH2
wherein each amino acid is in the L- configuration except for in Pbw3-D wherein each amino acid is in the D-configuration.
Each of the peptides of Lee consists of 9 amino acid residues in length and is therefore a nonameric peptide.
Each of the peptides of Lee comprises the dipeptide RR, which is a fragment of instant SEQ ID NO: 1.
Therefore, Lee teaches nonameric peptides represented by an amino acid sequence of SEQ ID NO: 1 (e.g. 9Pbw2, 9Pbw3, 9Pbw4) and an enantiomeric peptide thereof (e.g. Pbw3-D), satisfying all of the limitations of instant claim 1.
Regarding claims 2, 4, and 6, Lee teaches that the peptides have antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Salmonella typhimurium, Bacillus subtilis, Staphylococcus epidermidis, and Staphylococcus aureus (Table 2).
Regarding claim 8, Lee teaches that 9Pbw2 and 9Pbw4 did not show hemolytic activity and that 9Pbw3 and 9Pbw3-D did not show hemolytic activity at their MICs (Figure 1). Lee teaches that 9Pbw3-D did not show any cytotoxicity against the RAW264.7 cells up to 25 mM (Figure 2).
Regarding claim 9, Lee teaches that the peptides increase bacterial cell membrane permeability (Figure 7).
Regarding claim 12, Lee teaches that the enantiomeric peptide Pbw3-D is resistant to proteases (Figure 6).
Regarding claims 10 and 13, Lee teaches that the peptides inhibit activity of LPS via binding to LPS and suppress inflammation induced by LPS (Figures 5, 8).
Regarding claim 23, Lee teaches that the peptides can be used in a clinical application for antimicrobial therapy during Gram-negative bacterial infection (p. 681, conclusion).
Regarding claims 5, 7, and 11, Lee is silent regarding the claimed function of having activity against MDR gram-negative bacterial and carbapenem-resistant MDR gram-negative bacteria, and having activity against biofilm formation. Because the structure of the prior art peptides is the same as the claimed peptides, these functional effects are inherently met.
This rejection could be overcome by amending claim 1 to “A peptide consisting of the amino acid sequence of SEQ ID NO: 1 and the enantiomeric peptide thereof.”
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-13 and 26 are rejected under 35 U.S.C. 103 as being unpatentable over Lee (Enantiomeric 9-mer peptide analogs of protaetiamycine with bacterial cell selectivities and anti-inflammatory activities. Pept. Sci. 2011; 17: 675–682) in view of Cardodo (NPL 2, IDS 5/17/2024).
Determining the scope and contents of the prior art.
Lee teaches that protaetiamycine is an insect defensin, derived from the larvae of the beetle Protaetia brevitarsis (p. 676, col 1). Lee teaches a designed 9-mer peptide analog of protaetiamycine, 9Pbw3 (RLWLAIWRR-NH2), with high antimicrobial and anti-inflammatory activity as well as high cytotoxicity (p. 676, col 1). In order to improve 9Pbw3, Lee synthesized 9Pbw3-D, the all-D -amino acid analog of 9Pbw3 (p. 676, col 1; Table 1; Table 2). 9Pbw3-D showed less cytotoxicity against RAW264.7 cells as well as considerably stronger inhibition of NO production and inflammation-induced cytokine production in LPS-stimulated RAW264.7 cells than 9Pbw3 (Figures 2-4). 9Pbw3-D inhibited the gene expression of inflammatory-induced cytokine significantly more than 9Pbw3 (Figure 5) and showed high resistance to proteolytic digestion (Figure 6). Binding of 9Pbw3-D with LPS caused higher enhancement of the FITC fluorescence as a result of its stronger interaction with LPS compared to that of9Pbw3, consistent with their anti-inflammatory activities (Figure 8). Lee concludes that 9Pbw3-D with higher anti-inflammatory activity as well as lower cytotoxicity against mammalian cell compared to 9Pbw3 can be a potent noncytotoxic antibiotic candidate (p. 681, conclusion).
Ascertaining the differences between the prior art and the claims at issue.
Lee does not teach the retroinverse of 9Pbw3 or 9Pbw3-D, which are identical to instant SEQ ID NO: 1 and its enantiomeric peptide thereof (i.e. R-9Pbw3 and R-9Pbw3-D).
Resolving the level of ordinary skill in the pertinent art.
Cardoso teaches the design and engineering of partial D-amino acid, all D-amino acid, and retroinverso peptides for the development of antimicrobial peptides (Figure 5.1; Section 5.7).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to synthesize the retroinverse of 9Pbw3 or 9Pbw3-D (i.e. R-9Pbw3 and R-9Pbw3-D). The rationale for obviousness is use of known technique to improve similar devices (methods, or products) in the same way (MPEP § 2143.01(C)). The relevant findings for this rationale are as follows.
(1) The prior art contained a "base" product upon which the claimed invention can be seen as an "improvement". In the instant case, the primary reference Lee teaches the nonameric peptide 9Pbw3 (RLWLAIWRR-NH2) and its enantiomeric peptide 9Pbw3-D (Table 1) and demonstrate that both have antimicrobial and anti-inflammatory activity. 9Pbw3-D is an improvement of 9Pbw3 because the all-D enantiomeric peptide is protease resistant and has lower cytotoxicity (p. 681, conclusion). These peptides differ from the claimed peptides because instant SEQ ID NO: 1 and its enantiomer are retroinverso sequences of 9Pbw3 and 9Pbw3-D of Lee. The retroinverso peptides can be considered a further improvement of the prior art peptides. Therefore, prior art contained a "base" product upon which the claimed invention can be seen as an "improvement".
(2) The prior art contained a "comparable" device (method, or product that is not the same as the base device) that has been improved in the same way as the claimed invention. Cardoso teach that the design and engineering of partial D-amino acid, all D-amino acid, and retroinverso peptides for the development of antimicrobial peptides (Figure 5.1; Table 5.4). Cardoso disclose retroinverso derivatives of the antimicrobial host defense peptide IDR-1018 (p. 145). Several retroinverso peptides based on IDR-1018 were able to inhibit biofilm formation, including against multidrug resistant strains, with the retroinverso, all-D amino acid peptide showing the highest activity (p. 145). Cardoso also report that retroinverso derivatives of antimicrobial peptide BMAP28 exhibited antimicrobial activity and higher stability against proteases, as well as eliminated cytotoxicity and hemolytic activity of the parent peptide (p. 145). See section 5.7 and Table 5.4. Retroinverso synthesis is the same improvement that the instant claims represent compared to the primary reference Lee. Therefore, the prior art contained a "comparable" product that is not the same as the base product that has been improved in the same way as the claimed invention.
(3) One of ordinary skill in the art could have applied the known "improvement" technique in the same way to the "base" device (method, or product) and the results would have been predictable to one of ordinary skill in the art. One of ordinary skill in the art would expect that the retroinverso synthesis of Cardoso would improve the antimicrobial peptides of Lee because Cardoso teaches that retroinverso peptides exhibit resistance to enzymatic degradation, reduced hemolytic effects, and increases bioavailability (Figure 5.1) and have been used to improve other antimicrobial peptides (Section 5.7). Therefore, one of ordinary skill in the art could have applied the known "improvement" technique in the same way to the "base" product and the results would have been predictable to one of ordinary skill in the art.
(4) Whatever additional findings based on the Graham factual inquiries may be necessary, in view of the facts of the case under consideration, to explain a conclusion of obviousness. The specification compared the prior art peptides to the claimed peptides and found that R-Pro9-3D has better antimicrobial properties, LPS binding, antibiofilm properties, and proteolysis resistance than the other peptides (specification p. 42, lines 19-22). This effect is expected in view of the prior art of Cardoso, which discloses that retroinverso peptides in the prior art have exhibited this type of improvement (p. 145).
The rationale to support a conclusion that the claim would have been obvious is that a method of enhancing a particular class of devices (methods, or products) has been made part of the ordinary capabilities of one skilled in the art based upon the teaching of such improvement in other situations. One of ordinary skill in the art would have been capable of applying this known method of enhancement to a "base" device (method, or product) in the prior art and the results would have been predictable to one of ordinary skill in the art. "It's enough … to show that there was a known problem … in the art, that [another reference] … helped address that issue, and that combining the teachings of [the two references] wasn't beyond the skill of an ordinary artisan. Nothing more is required to show a motivation to combine under KSR." See Intel Corp. v. PACT XPP Schweiz AG, 61 F.4th 1373, 1380-81, 2023 USPQ2d 297 (Fed. Cir. 2023) (finding that both prior art references "address the same problem and that [the secondary reference’s] cache was a known way to address that problem is precisely the reason that there's a motivation to combine under KSR and our precedent.").
Therefore, a peptide consisting of instant SEQ ID NO: 1 and the enantiomeric peptide thereof is obvious over the prior art of Lee and Cardoso, satisfying all of the structural limitations of instant claims 1-13. All of the functional properties recited in claims 2-13 flow from following the suggestion in the cited art.
Regarding claim 23, it would have been obvious to use the peptides to treat gram-negative bacterial infection in view of the prior art of Lee which discloses this use for the parent peptide and the prior art of Cardoso which teaches improvement of antimicrobial peptides by retroinverso synthesis.
Therefore, claims 1-13 and 23 are obvious over the cited art.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHRISTINA MARCHETTI BRADLEY whose telephone number is (571)272-9044. The examiner can normally be reached Monday-Friday, 7 am - 3 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko G Garyu can be reached at (571) 270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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CHRISTINA MARCHETTI BRADLEY
Primary Examiner
Art Unit 1654
/CHRISTINA BRADLEY/Primary Examiner, Art Unit 1654
1 Hwang. Molecular Characterization of a Defensin-like Peptide from Larvae of a Beetle, Protaetia brevitarsis. Int. J. Indust. Entomol. Vol. 17, No. 1, 2008, pp. 131-135
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