Collagen Origami

Informacje na temat projektu

Collagen Origami

Identyfikator umowy o grant: 891009

DOI

10.3030/891009

Projekt został zamknięty

Data podpisania przez KE 5 Marca 2020

Data rozpoczęcia 1 Września 2020

Data zakończenia 31 Sierpnia 2022

Finansowanie w ramach

• EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions

Koszt całkowity

€ 203 149,44

Wkład UE

€ 203 149,44

Koordynowany przez

EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZUERICH
Switzerland

Periodic Reporting for period 1 - Collagen Origami (Collagen Origami)

Okres sprawozdawczy: 2020-09-01 do 2022-08-31

Podsumowanie kontekstu i ogólnych celów projektu

Collagen is the most abundant protein in mammals and the principal component of connective tissue. Mutations in collagen or its abnormal expression are associated with a number of diseases, e.g. the brittle bone disease or fibrosis. Collagen model peptides (CMPs) which mimic collagen’s intriguing triple-helical structure are used as synthetic surrogates to study this structural protein. In this project, we have shown that the functional groups at the ends of CMPs have a strong impact on the stability of collagen triple helices, a fact that has eluded the scientific community despite the more than 50-year history of CMPs.

Prace wykonane od początku projektu do końca okresu sprawozdawczego oraz najważniejsze dotychczasowe rezultaty

We have synthesized a series of CMPs with systematically varied terminal functional groups. We used a combined experimental and computational approach to elucidate the origins of the observed effects of the terminal groups on the peptide self-assembly. Our results revealed that the end-groups affect the stability of collagen triple helices by an interplay of two main effects: 1) strand preorganization, i.e. the ability of the individual peptides to pre-form a structure that is suitable for interacting with the other two strands; and 2) interstrand H-bonding, i.e. strengthening the interactions that hold the three strands together. We also show that the contributions of the end-groups are additive and can be used to predict the stability of collagen triple helices.

Innowacyjność oraz oczekiwany potencjalny wpływ (w tym dotychczasowe znaczenie społeczno-gospodarcze i szersze implikacje społeczne projektu)

The ability to rationally design CMPs with predictable properties is an indispensable tool for a multitude of applications. Our findings will guide the design of biological probes and drugs based on collagen hybridizing peptides as well as new synthetic collagen-based materials. Such probes and materials are being currently developed, e.g. as diagnostic tools to monitor tumor boundaries or treatments for chronic wounds. Our results will facilitate the design and implementation of these technologies.

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