Structural and mechanical behavior of type-I collagen fibrils in presence of induced electrostatic interactions through ionic liquids

Tuning the self-assembly of collagen has broad applications in the biomedical field owing to their desired biological performance as collagenous materials with tunable functionalities can further determine cellular responses. In this work, an attempt has been made to tune the self-assembly of collag...

Full description

Saved in:
Bibliographic Details
Published in:Biophysical chemistry 2024-04, Vol.307, p.107192-107192, Article 107192
Main Authors: Banerjee, Kuntala, Rasheeda, K., Tarannum, Aafiya, Fathima, N. Nishad
Format: Article
Language:English
Subjects:
Choline
Collagen
Collagen - chemistry
Collagen Type I - chemistry
Fibrillation
Ionic liquids
Ionic Liquids - chemistry
Phosphates
Self-assembly
Shear viscosity
Static Electricity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Tuning the self-assembly of collagen has broad applications in the biomedical field owing to their desired biological performance as collagenous materials with tunable functionalities can further determine cellular responses. In this work, an attempt has been made to tune the self-assembly of collagen using ionic liquids, viz., imidazolium chloride (IC) and choline dihydrogen phosphate (CDHP) at its physiological pH, followed by probing assembled systems using various characterization methods. Turbidity measurements of fibrillar networks were performed to ascertain the rate of fibril formation in addition of imidazolium chloride and choline dihydrogen phosphate to collagen at physiological pH. Morphological changes were examined using Scanning Electron Microscope (SEM), binding affinities were measured by Microscale Thermophoresis (MST), in addition to, changes in the shear viscosity, mechanical strength of collagen fibrils when interacted with imidazolium and choline based ILs were carried out using rotational rheometer and Quartz Crystal Microbalance (QCM) measurements. Experimental result depicts that CDHP imparts better crosslinking as well as mechanical strength compare to IC, which is already known for destabilizing the triple helix structure is inhibiting the fibril formation. This self-assembled, ionic-liquid treated collagen-fibrillar system would accelerate various force modulated fibrillar network study, for mimicking the ECM and tissue engineering application. [Display omitted] •Preparation of a tailor-made scaffold by tuned assembly of type-I collagen.•Stabilizing and destabilizing effects of ionic liquids on fibrillisation.•Molecular interaction studies by new techniques like MST, QCM.•Fibrillar interaction studies by Rheology, HR-SEM, Turbidity-Time assay.
ISSN:0301-4622
1873-4200
DOI:10.1016/j.bpc.2024.107192