Conformational study of peptoids

De Santis, Emiliana and Edwards, Alison A. (2012) Conformational study of peptoids. Chimica Oggi, 30 (5, S). pp. 32-36. ISSN 0392-839X. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Abstract

Peptides are ideal drug candidates due to their selectivity, however the therapeutic use of peptides is limited by their poor bioavailability e.g. due to the sensitivity to proteolytic enzymes. Therefore the development of peptidomimetic compounds is an area of research which has been rapidly expanding. The ability of such compounds (also known as foldamers) to fold into defined secondary structures is well documented and facilitates mimicry of the active conformation of peptide and proteins. A certain degree of flexibility is also desirable for peptidomimetics due to the importance of disorder in functional proteins. However, the greater flexibility complicates conformational studies due to the presence of multiple conformers e.g. NMR can have extensive signal overlap. In this scenario, chiroptical techniques such as circular dichroism become an invaluable tool for conformational studies.

Item Type: Article
Subjects: Q Science
Q Science > QD Chemistry
Q Science > QD Chemistry > Analytical Chemistry
Divisions: Faculties > Sciences > Medway School of Pharmacy
Depositing User: Alison Edwards
Date Deposited: 19 Apr 2017 11:14 UTC
Last Modified: 20 Apr 2017 08:58 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/45832 (The current URI for this page, for reference purposes)
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