Literature DB >> 26961970

A nanofiber assembly directed by the non-classical antiparallel β-structure from 4S-(OH) proline polypeptide.

Nitin D Bansode1, Mahesh V Sonar, Krishna N Ganesh.   

Abstract

The antiparallel arrangement of two strands of the non-classical β-structure, formed exclusively via cis-4S-(OH) prolyl polypeptide as established by FRET, propagates into self-assembled nanofibers upon conjugation with C12/C14/C16 hydrocarbon chains.

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Year:  2016        PMID： 26961970     DOI： 10.1039/c6cc00838k

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  2 in total

Review 1.  Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.

Authors:  Vincent P Gray; Connor D Amelung; Israt Jahan Duti; Emma G Laudermilch; Rachel A Letteri; Kyle J Lampe
Journal:  Acta Biomater       Date:  2021-10-25       Impact factor: 8.947

2.  Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units.

Authors:  Alexey B Mantsyzov; Oleg Y Savelyev; Polina M Ivantcova; Stefan Bräse; Konstantin V Kudryavtsev; Vladimir I Polshakov
Journal:  Front Chem       Date:  2018-03-28       Impact factor: 5.221
  2 in total

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