Using single molecule force spectroscopy to facilitate a rational design of Ca2+-responsive β-roll peptide-based hydrogels

2018 ◽  
Vol 6 (32) ◽  
pp. 5303-5312 ◽  
Author(s):  
Lichao Liu ◽  
Han Wang ◽  
Yueying Han ◽  
Shanshan Lv ◽  
Jianfeng Chen
Keyword(s):  
Mechanical Properties ◽  
Single Molecule ◽  
Rational Design ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy

Mechanical stability of Ca2+-responsive β-roll peptides (RTX) is largely responsible for the Ca2+-dependent mechanical properties of the RTX-based hydrogels.

scholarly journals Correction: Using single molecule force spectroscopy to facilitate a rational design of Ca2+-responsive β-roll peptide-based hydrogels

2020 ◽  
Vol 8 (20) ◽  
pp. 4527-4527
Author(s):  
Lichao Liu ◽  
Han Wang ◽  
Yueying Han ◽  
Shanshan Lv ◽  
Jianfeng Chen
Keyword(s):  
Single Molecule ◽  
Rational Design ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy

Correction for ‘Using single molecule force spectroscopy to facilitate a rational design of Ca2+-responsive β-roll peptide-based hydrogels’ by Lichao Liu et al., J. Mater. Chem. B, 2018, 6, 5303–5312, DOI: 10.1039/C8TB01511B.

scholarly journals Modulating mechanical stability of heterodimerization between engineered orthogonal helical domains

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Miao Yu ◽  
Zhihai Zhao ◽  
Zibo Chen ◽  
Shimin Le ◽  
Jie Yan
Keyword(s):  
Mechanical Properties ◽  
Single Molecule ◽  
Mechanical Stability ◽  
Functional Materials ◽  
Temperature Dependent ◽  
Single Molecule Force Spectroscopy ◽  
Protein Mechanics ◽  
Immunoglobulin Domain ◽  
Spectroscopy Studies ◽  
Spectrin Repeats

Abstract Mechanically stable specific heterodimerization between small protein domains have a wide scope of applications, from using as a molecular anchorage in single-molecule force spectroscopy studies of protein mechanics, to serving as force-bearing protein linker for modulation of mechanotransduction of cells, and potentially acting as a molecular crosslinker for functional materials. Here, we explore the possibility to develop heterodimerization system with a range of mechanical stability from a set of recently engineered helix-heterotetramers whose mechanical properties have yet to be characterized. We demonstrate this possibility using two randomly chosen helix-heterotetramers, showing that their mechanical properties can be modulated by changing the stretching geometry and the number of interacting helices. These helix-heterotetramers and their derivatives are sufficiently stable over physiological temperature range. Using it as mechanically stable anchorage, we demonstrate the applications in single-molecule manipulation studies of the temperature dependent unfolding and refolding of a titin immunoglobulin domain and α-actinin spectrin repeats.

Single molecule force spectroscopy reveals that the oxidation state of cobalt ions plays an important role in enhancing the mechanical stability of proteins

Nanoscale ◽  
2019 ◽  
Vol 11 (42) ◽  
pp. 19791-19796 ◽  
Author(s):  
Jiahao Xia ◽  
Jiacheng Zuo ◽  
Hongbin Li
Keyword(s):  
Oxidation State ◽  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Metal Chelation ◽  
Single Molecule Force Spectroscopy ◽  
Cobalt Ions

The binding of Co(iii) to the bi-histidine metal chelation site significantly enhances protein's mechanical stability.

scholarly journals Molecular mechanism of extreme mechanostability in a pathogen adhesin

Science ◽  
2018 ◽  
Vol 359 (6383) ◽  
pp. 1527-1533 ◽  
Author(s):  
Lukas F. Milles ◽  
Klaus Schulten ◽  
Hermann E. Gaub ◽  
Rafael C. Bernardi
Keyword(s):  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Covalent Bond ◽  
Binding Pocket ◽  
Peptide Backbone ◽  
Human Fibrinogen ◽  
Single Molecule Force Spectroscopy ◽  
Force Microscopy ◽  
Dynamics Simulations

High resilience to mechanical stress is key when pathogens adhere to their target and initiate infection. Using atomic force microscopy–based single-molecule force spectroscopy, we explored the mechanical stability of the prototypical staphylococcal adhesin SdrG, which targets a short peptide from human fibrinogen β. Steered molecular dynamics simulations revealed, and single-molecule force spectroscopy experiments confirmed, the mechanism by which this complex withstands forces of over 2 nanonewtons, a regime previously associated with the strength of a covalent bond. The target peptide, confined in a screwlike manner in the binding pocket of SdrG, distributes forces mainly toward the peptide backbone through an intricate hydrogen bond network. Thus, these adhesins can attach to their target with exceptionally resilient mechanostability, virtually independent of peptide side chains.

scholarly journals Mechanical stability of bivalent transition metal complexes analyzed by single-molecule force spectroscopy

2015 ◽  
Vol 11 ◽  
pp. 817-827 ◽  
Author(s):  
Manuel Gensler ◽  
Christian Eidamshaus ◽  
Maurice Taszarek ◽  
Hans-Ulrich Reissig ◽  
Jürgen P Rabe
Keyword(s):  
Transition Metal Complexes ◽  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Model Systems ◽  
Bond Rupture ◽  
Aqueous Environment ◽  
Single Molecule Force Spectroscopy ◽  
Bivalent Transition Metal ◽  
Rupture Behavior

Multivalent biomolecular interactions allow for a balanced interplay of mechanical stability and malleability, and nature makes widely use of it. For instance, systems of similar thermal stability may have very different rupture forces. Thus it is of paramount interest to study and understand the mechanical properties of multivalent systems through well-characterized model systems. We analyzed the rupture behavior of three different bivalent pyridine coordination complexes with Cu2+ in aqueous environment by single-molecule force spectroscopy. Those complexes share the same supramolecular interaction leading to similar thermal off-rates in the range of 0.09 and 0.36 s−1, compared to 1.7 s−1 for the monovalent complex. On the other hand, the backbones exhibit different flexibility, and we determined a broad range of rupture lengths between 0.3 and 1.1 nm, with higher most-probable rupture forces for the stiffer backbones. Interestingly, the medium-flexible connection has the highest rupture forces, whereas the ligands with highest and lowest rigidity seem to be prone to consecutive bond rupture. The presented approach allows separating bond and backbone effects in multivalent model systems.

Deciphering the Mechanical Properties of Type III Secretion System EspA Protein by Single Molecule Force Spectroscopy

Langmuir ◽  
2018 ◽  
Vol 34 (21) ◽  
pp. 6261-6270 ◽  
Author(s):  
Hila Nadler ◽  
Lihi Shaulov ◽  
Yossi Blitsman ◽  
Moran Mordechai ◽  
Jürgen Jopp ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Single Molecule ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Force Spectroscopy ◽  
Secretion System ◽  
Single Molecule Force Spectroscopy ◽  
Type Iii
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