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 .
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 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.
Election/Restrictions
It is noted that the applicant states, on page 11 of Applicant Arguments:
Without traversing the propriety of the restriction and election requirements, and solely for the purpose of advancing prosecution, applicant elects the following for examination:
Elected Invention Group: Group I, comprising claims directed to the peptide derivative of Formula (I), or a stereoisomer, mixture, cosmetically acceptable salt, or pharmaceutically acceptable salt thereof (claims 1-7).
Elected Species within Group I:
For the peptide derivative of Formula (I): Applicant elects the species wherein R₁ is
the substituent derived from nicotinic acid (NA) as shown in substituent (i) and R₂ is -OH. This elected species is exemplified in the specification as Peptide (1): NA-Pro-Lys-Glu-Lys-OH (see Examples 1-2). The biological data for this species is provided in Examples 6-8 and Figures 1-4.
For the preparation form (Claim 6): Applicant elects the species "emulsion" as the elected preparation form. This elected species is exemplified in the specification as Example 11.
For the delivery system (Claim 7): Applicant elects the species "liposome" as the elected delivery system, consistent with the examiner's indication during the telephone interview.
Applicant also argues regarding the species election:
With respect to the Examiner's requirement to elect one species, Applicant respectfully submits this election without prejudice. While Applicant has elected the aforementioned species to expedite the examination process, Applicant reserves all rights to challenge the Examiner's restriction requirement (including the propriety of the election itself) at a later stage, such as during an appeal or in response to any subsequent Office Action that improperly rejects claims drawn to non-elected species.
In accordance with the Manual of Patent Examining Procedure (MPEP), if the search and examination of all the claims in an application can be made without serious burden, the Examiner must examine them on the merits, even though they include claims to independent or distinct inventions. In the present case, the groups where R₂ is -OH and where R₂ is -NH₂ are closely related. A single prior art search would be sufficient to cover both species without imposing an undue burden on the Examiner. Therefore, Applicant submits that withdrawal of the restriction requirement is proper and respectfully requests that the Examiner withdraw the restriction requirement.
As such, as best understood by the Examiner, the applicant has elected Group I without traverse, and the species both without traverse (“Without traversing the propriety of the restriction and election requirements”) and with traverse since applicant has presented an argument regarding burden.
Applicant's election with traverse of R2 = OH of peptide of Formula I is questioned, but acknowledged. The traversal is on the ground(s) that R2 = OH and R2 = NH2 present no search burden. This is not found persuasive because it is known in the art that peptides with a terminal OH and peptides with a terminal NH2 have differing physical and in vivo properties, and therefore must be searched separately. See the “Introduction” section of Bokatzian-Johnson (“A Comparison of the Effects of Amide and Acid Groups at the C-Terminus on the Collision-Induced Dissociation of Deprotonated Peptides,” J. Am. Soc. Mass Spectrom. (2012) 23: 1544-1557; attached).
The requirement is still deemed proper and is therefore made FINAL.
Claims 1-3 and 6-19 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions, there being no allowable generic or linking claim.
Claim Status
Claims 20-22 are newly added.
Claims 1-22 are pending.
Claims 1-3 and 6-19 are withdrawn.
Claims 4-5 and 20-22 are examined on the merits in this prosecution.
CLAIM REJECTIONS
Obviousness Rejection
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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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.
1) Claims 5, 20, and 21, are rejected under 35 U.S.C. 103 as being unpatentable over Choi (US 9,456.972), in view of Farwick (US 2012/0244094 A1).
For claim 20, Choi teaches niacin-peptide which has skin whitening activity. The peptide of the present invention has skin whitening activity by inhibiting melanogenesis, that is, by inhibiting the expression of a gene related to melanogenesis (for example, TRP-1, TRP-2, or MIFT). The peptides taught by Choi have high stability and skin permeability, and range from 2 to 6 amino acids (see SEQ ID NOs 1-55, columns 14-37). Choi further teaches cosmetic compositions for skin whitening which contains the niacin-peptide (Abstract). It is noted that niacin is an alternative term for nicotinate.
Choi teaches niacinamide has been suggested to only block movement of melanosomes onto the skin surface. It has been well-known for maintenance of bright skin by decreasing melanin movement from melanocytes to keratinocytes (col 2: 4-14). Choi teaches the object of the invention is to provide niacin-peptides having a skin whitening effect (col 2: 42-43).
For claim 5, Choi teaches:
PNG
media_image1.png
126
419
media_image1.png
Greyscale
For claim 21 (dependent on claim 5), Choi teaches the cosmetic composition in the form of an emulsion (col 5: 55-57).
Choi does not teach the Pro-Lys-Glu-Lys peptide recited in claim 20.
Farwick teaches the missing element of Choi.
Farwick teaches “the use of the tetrapeptide PKEK [Pro-Lys-Glu-Lys] or one of its derivatives for lightening the color of human skin, for bleaching pigment spots and/or for evening out irregularities in skin coloration” (pg 1, [0014]).
The skilled artisan would have a reasonable expectation of success in substituting Farwick's Pro-Lys-Glu-Lys for the 2-6 residue peptides in Choi’s skin-lightening composition because Choi teaches certain niacin- (e.g. nicotinate-) substituted peptides comprising 2-6 amino acids are useful in cosmetics for the purposes of skin whitening and Farwick teaches that Pro-Lys-Glu-Lys peptide is a skin whitening or lightening agent. The skilled artisan could have substituted one compound for another because Choi and Farwick each teach that the respective peptides were both suitable for application to the to the skin for skin lightening. The person of ordinary skill in the art would have found it obvious to make the substitution because ordinarily skilled artisans would have predicted that nicotinate-Pro-Lys-Glu-Lys peptide would be safe and effective based on the compounds' shared activity.
2) Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Choi (cited above), in view of Farwick (cited above) and Serajuddin (“Salt formation to improve drug solubility,” Advanced Drug Delivery Reviews 59 (2007) 603–616).
The teaching of Choi and Farwick are discussed above.
The combination of Choi and Farwick does not teach a metal salt of the tetrapeptide such as a sodium salt.
For claim 4, the formation of a physiologically non-toxic metal salt of a peptide, such as a sodium salt, is well-known in the art as a means of improving peptide or acid solubility and absorption, as taught by Serajuddin (pg 604, “Introduction”).
The skilled artisan would have expected success in substituting the niacin-substituted peptide sodium salt taught by Sarajuddin for the peptide carboxylic acid taught by the combination of Choi and Farwick because Sarajuddin teaches that carboxylate salts of peptides are easily formed and have improved solubility and absorption properties.
3) Claim 22 is rejected under 35 U.S.C. 103 as being unpatentable over Choi (cited above), in view of Farwick (cited above) and Dreher (US 2014/0309173 A1).
The teaching of Choi and Farwick are discussed above.
The combination of Choi and Farwick does not teach a liposomal formulation of the N-substituted Pro-Lys-Glu-Lys tetrapeptide.
Dreher teaches the missing element of the combination of Choi and Farwick.
Dreher teaches tetrapeptides, N-substituted with acyl groups are particularly suited for topical applications (pgs 4-5, [0054]). It is noted that Dreher does not specifically teach nicotinate substitution, but teaches acyl and octanoyl peptide substitution ([0054]-[0055]). Dreher teaches the compositions may be prepared in the form of liposomes (pg 29, [0302]).
The person of ordinary skill would have had a reasonable expectation of success in selecting a liposomal delivery system for the niacin-substituted Pro-Lys-Glu-Lys tetrapeptide taught by the combination of Choi and Farwick because Dreher teaches liposomal formulations are useful for the topical application of a variety of acyl-substituted tetrapeptides (pg 2, [0020]).
CONCLUSION
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MICHAEL P COHEN whose telephone number is (571)270-7402. The examiner can normally be reached on M-Th 8:30-5:30; F 9-4.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sahana S. Kaup, can be reached on (571) 272-6897. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/MICHAEL P COHEN/Primary Examiner, Art Unit 1612
Prosecution Insights