Single Molecule Force Spectroscopy Reveals Critical Roles of Hydrophobic Core Packing in Determining the Mechanical Stability of Protein GB1

Langmuir ◽  
2012 ◽  
Vol 28 (33) ◽  
pp. 12319-12325 ◽  
Author(s):  
Tianjia Bu ◽  
Hui-Chuan Eileen Wang ◽  
Hongbin Li
Keyword(s):  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Hydrophobic Core ◽  
Single Molecule Force Spectroscopy ◽  
Core Packing ◽  
Protein Gb1

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.

scholarly journals Structural Determinants of Coiled Coil Mechanics

2019 ◽  
Author(s):  
Patricia Lopez-Garcia ◽  
Melis Goktas ◽  
Ana E. Bergues-Pupo ◽  
Beate Koksch ◽  
Daniel Varon Silva ◽  
...  
Keyword(s):  
Transition State ◽  
Single Molecule ◽  
Mechanical Stability ◽  
Coiled Coil ◽  
Building Blocks ◽  
Shear Loading ◽  
Hydrophobic Core ◽  
Structural Determinants ◽  
Helix Propensity ◽  
Core Packing

The natural abundance of coiled coil (CC) motifs in the cytoskeleton and the extracellular matrix suggests that CCs play a crucial role in the bidirectional mechanobiochemical signaling between cells and the matrix. Their functional importance and structural simplicity has allowed the development of numerous applications, such as protein-origami structures, drug delivery systems and biomaterials. With the goal of establishing CCs as nanomechanical building blocks, we investigated the importance of helix propensity and hydrophobic core packing on the mechanical stability of 4-heptad CC heterodimers. Using single-molecule force spectroscopy, we show that both parameters determine the force-induced dissociation in shear loading geometry; however, with different effects on the energy landscape. Decreasing the helix propensity lowers the transition barrier height, leading to a concomitant decrease in the distance to the transition state. In contrast, a less tightly packed hydrophobic core increases the distance to the transition state. We propose that this sequence-structure-mechanics relationship is evolutionarily optimized in natural CCs and can be used for tuning their mechanical properties in applications.

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.

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