Isotope-Edited Vibrational Circular Dichroism Study Reveals a Flexible N-Terminal Structure of Islet Amyloid Peptide (NFGAIL) in Amyloid Fibril Form: A Site-Specific Local Structural Analysis

Autor: Anagha C, Unnikrishnan, Ganesh, Shanmugam
Rok vydání: 2022
Předmět:
Zdroj: SSRN Electronic Journal.
ISSN: 1556-5068
DOI: 10.2139/ssrn.4215784
Popis: The short peptide fragment NFGAIL (IAPf) is a well-known amyloidogenic peptide (22-27), derived from human islet amyloid polypeptide(hIAPP), whose fibrillar structure is often used to better understand the wild-type hIAPP amyloid fibrils, associated with type II diabetes. Despite an extensive study, the fibrillar structure of IAPf at the amino acid residue level is still unclear. Herein, the vibrational circular dichroism(VCD) spectroscopic technique coupled with isotope labelling strategy has been used to study the site-specific local structure of IAPf amyloid fibrils. Two
Databáze: OpenAIRE