Nanomechanical Contribution of Collagen and von Willebrand Factor A in Marine Underwater Adhesion and Its Implication for Collagen Manipulation

Hee Young Yoo; Jun Huang; Lin Li; Mathias Foo; Hongbo Zeng; Dong Soo Hwang

doi:10.1021/acs.biomac.5b01622

Nanomechanical Contribution of Collagen and von Willebrand Factor A in Marine Underwater Adhesion and Its Implication for Collagen Manipulation

Hee Young Yoo, Jun Huang, Lin Li, Mathias Foo, Hongbo Zeng, Dong Soo Hwang

School of Mechanical, Aerospace and Automotive Engineering

Research output: Contribution to journal › Article

7 Citations (Scopus)

11 Downloads (Pure)

Abstract

Recent works on mussel adhesion have identified a load bearing matrix protein (PTMP1) containing von Willebrand factor (vWF) with collagen binding capability that contributes to the mussel holdfast by manipulating mussel collagens. Using a surface forces apparatus, we investigate for the first time, the nanomechanical properties of vWF-collagen interaction using homologous proteins of mussel byssus, PTMP1 and preCollagens (preCols), as collagen. Mimicking conditions similar to mussel byssus secretion (pH <5.0) and seawater condition (pH 8.0), PTMP1 and preCol interact weakly in the "positioning" phase based on vWF-collagen binding and strengthen in "locked" phase due to the combined effects of electrostatic attraction, metal binding, and mechanical shearing. The progressive enhancement of binding between PTMP1 with porcine collagen under the aforementioned conditions is also observed. The binding mechanisms of PTMP1-preCols provide insights into the molecular interaction of the mammalian collagen system and the development of an artificial extracellular matrix based on collagens.

Original language	English
Pages (from-to)	946-953
Number of pages	8
Journal	Biomacromolecules
Volume	17
Issue number	3
Early online date	19 Feb 2016
DOIs	https://doi.org/10.1021/acs.biomac.5b01622
Publication status	Published - 14 Mar 2016

Bibliographical note

Copyright © and Moral Rights are retained by the author(s) and/ or other copyright owners. A copy can be downloaded for personal non-commercial research or study, without prior permission or charge. This item cannot be reproduced or quoted extensively from without first obtaining permission in writing from the copyright holder(s). The content must not be changed in any way or sold commercially in any format or medium without the formal permission of the copyright holders.

Keywords

Proximal thread matrix protein-1;
Nanomechanics
von Willebrand factor (vWF);
Tissue engineering
Mussel adhesion
Shear effect

Access to Document

10.1021/acs.biomac.5b01622

Post-printAccepted author manuscript, 1.34 MBLicence: CC BY-NC

Fingerprint Dive into the research topics of 'Nanomechanical Contribution of Collagen and von Willebrand Factor A in Marine Underwater Adhesion and Its Implication for Collagen Manipulation'. Together they form a unique fingerprint.

Cite this

Yoo, H. Y., Huang, J., Li, L., Foo, M., Zeng, H., & Hwang, D. S. (2016). Nanomechanical Contribution of Collagen and von Willebrand Factor A in Marine Underwater Adhesion and Its Implication for Collagen Manipulation. Biomacromolecules, 17(3), 946-953. https://doi.org/10.1021/acs.biomac.5b01622

@article{35f1fb8f2f7247bb90cb894aad710ee8,

title = "Nanomechanical Contribution of Collagen and von Willebrand Factor A in Marine Underwater Adhesion and Its Implication for Collagen Manipulation",

abstract = "Recent works on mussel adhesion have identified a load bearing matrix protein (PTMP1) containing von Willebrand factor (vWF) with collagen binding capability that contributes to the mussel holdfast by manipulating mussel collagens. Using a surface forces apparatus, we investigate for the first time, the nanomechanical properties of vWF-collagen interaction using homologous proteins of mussel byssus, PTMP1 and preCollagens (preCols), as collagen. Mimicking conditions similar to mussel byssus secretion (pH <5.0) and seawater condition (pH 8.0), PTMP1 and preCol interact weakly in the {"}positioning{"} phase based on vWF-collagen binding and strengthen in {"}locked{"} phase due to the combined effects of electrostatic attraction, metal binding, and mechanical shearing. The progressive enhancement of binding between PTMP1 with porcine collagen under the aforementioned conditions is also observed. The binding mechanisms of PTMP1-preCols provide insights into the molecular interaction of the mammalian collagen system and the development of an artificial extracellular matrix based on collagens.",

keywords = "Proximal thread matrix protein-1;, Nanomechanics, von Willebrand factor (vWF);, Tissue engineering, Mussel adhesion, Shear effect",

author = "Yoo, {Hee Young} and Jun Huang and Lin Li and Mathias Foo and Hongbo Zeng and Hwang, {Dong Soo}",

note = "Copyright {\circledC} and Moral Rights are retained by the author(s) and/ or other copyright owners. A copy can be downloaded for personal non-commercial research or study, without prior permission or charge. This item cannot be reproduced or quoted extensively from without first obtaining permission in writing from the copyright holder(s). The content must not be changed in any way or sold commercially in any format or medium without the formal permission of the copyright holders.",

year = "2016",

month = "3",

day = "14",

doi = "10.1021/acs.biomac.5b01622",

language = "English",

volume = "17",

pages = "946--953",

journal = "Biomacromolecules",

issn = "1525-7797",

publisher = "American Chemical Society",

number = "3",

}

TY - JOUR

T1 - Nanomechanical Contribution of Collagen and von Willebrand Factor A in Marine Underwater Adhesion and Its Implication for Collagen Manipulation

AU - Yoo, Hee Young

AU - Huang, Jun

AU - Li, Lin

AU - Foo, Mathias

AU - Zeng, Hongbo

AU - Hwang, Dong Soo

N1 - Copyright © and Moral Rights are retained by the author(s) and/ or other copyright owners. A copy can be downloaded for personal non-commercial research or study, without prior permission or charge. This item cannot be reproduced or quoted extensively from without first obtaining permission in writing from the copyright holder(s). The content must not be changed in any way or sold commercially in any format or medium without the formal permission of the copyright holders.

PY - 2016/3/14

Y1 - 2016/3/14

N2 - Recent works on mussel adhesion have identified a load bearing matrix protein (PTMP1) containing von Willebrand factor (vWF) with collagen binding capability that contributes to the mussel holdfast by manipulating mussel collagens. Using a surface forces apparatus, we investigate for the first time, the nanomechanical properties of vWF-collagen interaction using homologous proteins of mussel byssus, PTMP1 and preCollagens (preCols), as collagen. Mimicking conditions similar to mussel byssus secretion (pH <5.0) and seawater condition (pH 8.0), PTMP1 and preCol interact weakly in the "positioning" phase based on vWF-collagen binding and strengthen in "locked" phase due to the combined effects of electrostatic attraction, metal binding, and mechanical shearing. The progressive enhancement of binding between PTMP1 with porcine collagen under the aforementioned conditions is also observed. The binding mechanisms of PTMP1-preCols provide insights into the molecular interaction of the mammalian collagen system and the development of an artificial extracellular matrix based on collagens.

AB - Recent works on mussel adhesion have identified a load bearing matrix protein (PTMP1) containing von Willebrand factor (vWF) with collagen binding capability that contributes to the mussel holdfast by manipulating mussel collagens. Using a surface forces apparatus, we investigate for the first time, the nanomechanical properties of vWF-collagen interaction using homologous proteins of mussel byssus, PTMP1 and preCollagens (preCols), as collagen. Mimicking conditions similar to mussel byssus secretion (pH <5.0) and seawater condition (pH 8.0), PTMP1 and preCol interact weakly in the "positioning" phase based on vWF-collagen binding and strengthen in "locked" phase due to the combined effects of electrostatic attraction, metal binding, and mechanical shearing. The progressive enhancement of binding between PTMP1 with porcine collagen under the aforementioned conditions is also observed. The binding mechanisms of PTMP1-preCols provide insights into the molecular interaction of the mammalian collagen system and the development of an artificial extracellular matrix based on collagens.

KW - Proximal thread matrix protein-1;

KW - Nanomechanics

KW - von Willebrand factor (vWF);

KW - Tissue engineering

KW - Mussel adhesion

KW - Shear effect

U2 - 10.1021/acs.biomac.5b01622

DO - 10.1021/acs.biomac.5b01622

M3 - Article

C2 - 26894593

VL - 17

SP - 946

EP - 953

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 3

ER -