Effect of hydrophilic or hydrophobic interactions on the self-assembly behavior and micro-morphology of a collagen mimetic peptide

Xiaomin Luo,Ying Liu,Xinhua Liu,Qianqian Huo,Chi Zheng

doi:10.1186/s42825-021-00054-3

Xiaomin Luo, Ying Liu + Show 3 more

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https://doi.org/10.1186/s42825-021-00054-3

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Abstract

Peptide self-assembles with bionic properties have been widely utilized for bioactive drugs and biomedical materials. Collagen mimetic peptide (CMP) gains more attention due to its unique advantages in biosecurity and function. Unfortunately, the self-assembly mechanism of CMP, particularly the effect of intermolecular forces on its self-assembly behavior and morphology, is still unrecognized. Herein, the hydrophilic glycidol (GCD) and hydrophobic Y-glycidyl ether oxypropyl trimethoxysilane (GLH) were grafted onto the side chains of CMP through the ring-opening reaction (GCD/CMP, GLH/CMP). Subsequently, the effects of hydrophilic and hydrophobic interactions on the self-assembly behavior and morphology of CMP were further studied. The results substantiated that the GCD/CMP and GLH/CMP self-assembly followed “nucleation-growth” mechanism, and the supererogatory hydrophilic and hydrophobic groups prolonged the nucleation and growth time of CMP self-assembly. Noted that the hydrophilic interaction had stronger driving effects than hydrophobic interaction on the self-assembly of CMP. The GCD/CMP and GLH/CMP self-assembles exhibited fibrous 3D network and microsphere morphology, respectively. Furthermore, the GLH/CMP self-assembles had better resistance to degradation. Consequently, the microtopography and degradation properties of CMP self-assembles could be controlled by the hydrophilic and hydrophobic interactions between CMP, which would further provide a way for subsequent purposeful design of biomedical materials.Graphical abstract

Highlights

Polypeptide is recognized as one of the most promising natural organic polymer in the field of biomedical materials due to its analogous nature to ECM [1,2,3]
The preparation conditions of GCD/ Collagen mimetic peptide (CMP) and glycidyl ether oxypropyl trimethoxysilane (GLH)/CMP were optimized based on the amino conversion rate (Fig. 1d), which implies that the optimal reaction conditions are 1:1 of the amino group and epoxy group molar ratio, 12 h of reaction time, 37 °C of temperature, pH 10.0
4 Conclusions The objective of this study is to evaluate the selfassembly mechanism of CMP, the effect of hydrophilic and hydrophobic interactions between CMP bulk on its self-assembly behavior and morphology by grafting the hydrophilic GCD and hydrophobic GLH onto the side chains of CMP through the ring-opening reaction

Summary

Introduction

Polypeptide is recognized as one of the most promising natural organic polymer in the field of biomedical materials due to its analogous nature to ECM [1,2,3]. Polypeptide molecules can self-assemble into more ordered aggregates in nature with bionic structures, diverse functions and wide-ranging applications through non-covalent interactions, which make it more potential in the development of bioactive peptide drugs and biomedical materials [18,19,20,21,22,23]. The understanding of self-assembly behavior of polypeptide could contribute to regulate the anticipatory properties of the aggregated materials at the molecular level to meet various practical applications [28, 29]. The current research on CMP and its assembly system is in the primary research stage in terms of structural complexity, multi-level, functionality, and application, especially the study on its assembly behavior is still blank

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