Insulin amyloid fibril formation reduction by tripeptide stereoisomers

Author:

Rosetti Beatrice1ORCID,Kralj Slavko23ORCID,Scarel Erica1ORCID,Adorinni Simone1ORCID,Rossi Barbara4ORCID,Vargiu Attilio V.5ORCID,Garcia Ana M.6ORCID,Marchesan Silvia1ORCID

Affiliation:

1. Chemical Pharmaceutical Science Department, University of Trieste, 34127 Trieste, Italy

2. Materials Synthesis Department, Jožef Stefan, Institute, 1000 Ljubljana, Slovenia

3. Department of Pharmaceutical Technology, Faculty of Pharmacy, University of Ljubljana, 1000 Ljubljana, Slovenia

4. Elettra Sincrotrone Trieste, Strada Statale 14 - km 163,5 Basovizza, 34149 Trieste, Italy

5. Physics Department, University of Cagliari, 09042 Monserrato, Cagliari, Italy

6. Facultad de Ciencias y Tecnologías Químicas, Instituto Regional de Investigación Científica Aplicada (IRICA), Universidad de Castilla-La Mancha, 13071 Ciudad Real, Spain

Abstract

A simple tripeptide significantly reduces insulin amyloid fibril formation and it is proposed as a formulation stabiliser. In silico studies reveal the mechanism of interaction with the insulin hydrophobic motifs that are prone to fibrillation.

Funder

Fondazione Cassa di Risparmio di Pistoia e Pescia

Elettra-Sincrotrone Trieste

Junta de Comunidades de Castilla-La Mancha

Università degli Studi di Trieste

Fondazione di Sardegna

Publisher

Royal Society of Chemistry (RSC)

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