Structure and Function of Ion Pumps Studied by Atomic Force Microscopy and Gene-transfer Experiments Using Chimeric Na+/K+- and Ca2+ ATPases

A widely accepted tenet of biomaterials research is that the initial step following contact of a synthetic material with blood is the rapid adsorption of plasma proteins. The composition of this adsorbed protein layer is dependent on a variety of factors, including the surface properties of the implant material and the nature of the adsorbing proteins, and the composition and function of this protein layer is important in the subsequent biological response and ultimately the success or failure of the implanted material. While a great amount of effort has gone into developing structure/function responses for implanted biomaterials, there is still much about the molecular level interactions to be determined. We utilized atomic force microscopy (AFM) to investigate the molecular-level interactions of proteins with model biomaterial substrates. The AFM is unique in that it offers the opportunity to characterize interfacial environments, determine material properties, measure protein/surface interaction forces, and visualize the tertiary structure of adsorbed proteins.

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Nanoscale Analysis of the Effect of Pathogenic Mutations on Polycystin-1

ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology ◽

10.1115/nemb2010-13093 ◽

2010 ◽

Author(s):

Liang Ma ◽

Meixiang Xu ◽

Andres F. Oberhauser

Keyword(s):

Single Molecule ◽

Conformational Changes ◽

Protein Interactions ◽

Structure And Function ◽

Eukaryotic Cells ◽

Mechanical Forces ◽

Force Microscopy ◽

Physiological Conditions ◽

Atomic Force ◽

And Function

The activity of proteins and their complexes often involves the conversion of chemical energy (stored or supplied) into mechanical work through conformational changes. Mechanical forces are also crucial for the regulation of the structure and function of cells and tissues. Thus, the shape of eukaryotic cells is the result of cycles of mechano-sensing, mechano-transduction, and mechano-response. Recently developed single-molecule atomic force microscopy (AFM) techniques can be used to manipulate single molecules, both in real time and under physiological conditions, and are ideally suited to directly quantify the forces involved in both intra- and intermolecular protein interactions. In combination with molecular biology and computer simulations, these techniques have been applied to characterize the unfolding and refolding reactions in a variety of proteins, such as titin (an elastic mechano-sensing protein found in muscle) and polycystin-1 (PC1, a mechanosensor found in the kidney).

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Review of Progress in Atomic Force Microscopy

The Open Neuroimaging Journal ◽

10.2174/1874440001812010086 ◽

2018 ◽

Vol 12 (1) ◽

pp. 86-104 ◽

Cited By ~ 1

Author(s):

S. Maghsoudy-Louyeh ◽

M. Kropf ◽

B. R. Tittmann

Keyword(s):

Atomic Force Microscopy ◽

Biological Samples ◽

Underlying Structure ◽

Force Microscopy ◽

Atomic Force ◽

Cell Structures ◽

Resolution Imaging ◽

Recent Trends ◽

Software And Hardware ◽

And Function

The study of biological samples is one of the most attractive and innovative fields of application of atomic force microscopy AFM. Recent breakthroughs in software and hardware have revolutionized this field and this paper reports on recent trends and describes examples of applications on biological samples. Originally developed for high-resolution imaging purposes, the AFM also has unique capabilities as a nano-indentor to probe the dynamic visco-elastic material properties of living cells in culture. In particular, AFM elastography combines imaging and indentation modalities to map the spatial distribution of cell mechanical properties, which in turn reflect the structure and function of the underlying structure. This paper describes the progress and development of atomic force microscopy as applied to animal and plant cell structures.

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Biological physics by high-speed atomic force microscopy

Philosophical Transactions of The Royal Society A Mathematical Physical and Engineering Sciences ◽

10.1098/rsta.2019.0604 ◽

2020 ◽

Vol 378 (2186) ◽

pp. 20190604 ◽

Cited By ~ 1

Author(s):

Ignacio Casuso ◽

Lorena Redondo-Morata ◽

Felix Rico

Keyword(s):

Atomic Force Microscopy ◽

Molecular Motors ◽

High Speed ◽

Structural Information ◽

Biological Systems ◽

Force Microscopy ◽

Atomic Force ◽

Biological Physics ◽

And Function ◽

Physical Phenomena

While many fields have contributed to biological physics, nanotechnology offers a new scale of observation. High-speed atomic force microscopy (HS-AFM) provides nanometre structural information and dynamics with subsecond resolution of biological systems. Moreover, HS-AFM allows us to measure piconewton forces within microseconds giving access to unexplored, fast biophysical processes. Thus, HS-AFM provides a tool to nourish biological physics through the observation of emergent physical phenomena in biological systems. In this review, we present an overview of the contribution of HS-AFM, both in imaging and force spectroscopy modes, to the field of biological physics. We focus on examples in which HS-AFM observations on membrane remodelling, molecular motors or the unfolding of proteins have stimulated the development of novel theories or the emergence of new concepts. We finally provide expected applications and developments of HS-AFM that we believe will continue contributing to our understanding of nature, by serving to the dialogue between biology and physics. This article is part of a discussion meeting issue ‘Dynamic in situ microscopy relating structure and function’.

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Effect of cholesterol and amyloid-β peptide on structure and function of mixed-lipid films and pulmonary surfactant BLES: an atomic force microscopy study

Nanomedicine Nanotechnology Biology and Medicine ◽

10.1016/j.nano.2010.05.001 ◽

2010 ◽

Vol 6 (6) ◽

pp. 808-814 ◽

Cited By ~ 8

Author(s):

Francis Hane ◽

Elizabeth Drolle ◽

Zoya Leonenko

Keyword(s):

Pulmonary Surfactant ◽

Amyloid Β ◽

Microscopy Study ◽

Structure And Function ◽

Amyloid Β Peptide ◽

Atomic Force Microscopy Study ◽

Force Microscopy ◽

Atomic Force ◽

Lipid Films ◽

And Function

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