Open Access Research Article Article ID: IJNNN-2-109

    Design of Peptide Models for β-Hairpins and Equilibrating Helix-Hairpin Structures

    Chinnasamy Selvakkumar*, Eashwarwark Vikram Reddy, Kesavanarayanan Krishnan Selvarajan, Nazeerullah Rahamuthullah and Muftha Mohamed Zarmouh

    It is well established that synthetic peptides containing a centrally positioned Type-I or Type-II β-turn can form well folded peptide hairpins (1). Earlier studies from this laboratory have established that D-Pro-Xxx segments nucleate β-hairpin structures, with formation of a central Type-II β-turn (2). The octapeptide (Boc-Leu-Phe-Val-Aib-D-Ala-Leu-Phe- Val-OMe) is a rare example of a synthetic peptide hairpin, containing a central Type-I β-turn. Hairpins with Type-I turns are considerably more twisted than their Type-II counterparts. The Aib-Xxx segment has also been shown to adopt a Type-I β-turn structure, resulting in incorporation into the centre of a long synthetic, helical peptide (3) (Figures 1,2). 


    Published on: May 4, 2016 Pages: 15-17

    Full Text PDF Full Text HTML DOI: 10.17352/2455-3492.000009
    CrossMark Publons Harvard Library HOLLIS Search IT Semantic Scholar Get Citation Base Search Scilit OAI-PMH ResearchGate Academic Microsoft GrowKudos Universite de Paris UW Libraries SJSU King Library SJSU King Library NUS Library McGill DET KGL BIBLiOTEK JCU Discovery Universidad De Lima WorldCat VU on WorldCat


    Global Views

    Case Reports

    Peertechz Tweets

    Pinterest on IJNNN

    Help ? Google Reviews 11