Ultrahigh Adhesion Force Between Silica-Binding Peptide SB7 and Glass Substrate Studied by Single-Molecule Force Spectroscopy and Molecular Dynamic Simulation

Zhang, Xiaoxu; Chen, Jialin; Li, Enci; Hu, Chunguang; Luo, Shi-Zhong; He, Chengzhi

doi:10.3389/fchem.2020.600918

Cited by 21 publications

(12 citation statements)

References 44 publications

(53 reference statements)

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“…Functionalization of AFM probes and substrates. The surface functionalization was performed as described previously 21,35,36 . Briefly, The MLCT-Bio-DC AFM probes (Bruker) and glass substrates were immersed in 50 % isopropanol for 5 mins, cleaned in a UV radiation and ozone (UV-O) cleaner and silanized with (3-aminopropyl)-triethoxysilane (APTES).…”

Section: Methodsmentioning

confidence: 99%

Pathogen-Host Adhesion between SARS-CoV-2 Spike Proteins from Different Variants and Human ACE2 Probed at Single-Molecule and Single-Cell Levels

Zhang

Chen

Hong

et al. 2022

Preprint

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Pathogen-Host adhesion is considered the first step of infection for many pathogens such as bacteria and virus. The binding of the receptor binding domain (RBD) of SARS-CoV-2 Spike protein (S protein) onto human angiotensin-converting enzyme 2 (ACE2) is considered as the first step for the SARS-CoV-2 to adhere onto the host cells during the infection. Within three years, a number of variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have been found all around the world. Here, we investigated the adhesion of S Proteins from different variants and ACE2 using atomic force microscopy (AFM)-based single-molecule force spectroscopy (SMFS) and single-cell force spectroscopy (SCFS). We found that the unbinding force and binding probability of the S protein from Delta variant to the ACE2 was the highest among the variants tested in our study at both single-molecule and single-cell levels. Molecular dynamics simulation showed that ACE2-RBD (Omicron) complex is destabilized by the E484A and Y505H mutations and stabilized by S477N and N501Y mutations, when compared with Delta variant. In addition, a neutralizing antibody, produced by immunization with wild type RBD of S protein, could effectively inhibit the binding of S proteins from wild type, Delta and Omicron variants onto ACE2. Our results provide new insight for the molecular mechanism of the adhesive interactions between S protein and ACE2 and suggest effective monoclonal antibody can be prepared using wild type S protein against the Delta and Omicron variants by inhibit the pathogen-host adhesion.

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Section: Methodsmentioning

confidence: 99%

Pathogen-Host Adhesion between SARS-CoV-2 Spike Proteins from Different Variants and Human ACE2 Probed at Single-Molecule and Single-Cell Levels

Zhang

Chen

Hong

et al. 2022

Preprint

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“…To examine the linker effect, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the mechanical stability of human Ig domains. SMFS can manipulate a single molecule mechanically [ 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 ] and AFM-SMFS has been widely used to study the mechanical stability of proteins [ 23 , 24 , 25 , 26 , 27 , 28 , 29 ], protein-protein interactions [ 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 ], and chemical bonds [ 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 ]. Many titin domains have been studied [ 57 , 58 , 59 ].…”

Section: Introductionmentioning

confidence: 99%

Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin

Tong

Tian

Zheng

2022

IJMS

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Titin is the largest protein in humans, composed of more than one hundred immunoglobulin (Ig) domains, and plays a critical role in muscle’s passive elasticity. Thus, the molecular design of this giant polyprotein is responsible for its mechanical function. Interestingly, most of these Ig domains are connected directly with very few interdomain residues/linker, which suggests such a design is necessary for its mechanical stability. To understand this design, we chose six representative Ig domains in titin and added nine glycine residues (9G) as an artificial interdomain linker between these Ig domains. We measured their mechanical stabilities using atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) and compared them to the natural sequence. The AFM results showed that the linker affected the mechanical stability of Ig domains. The linker mostly reduces its mechanical stability to a moderate extent, but the opposite situation can happen. Thus, this effect is very complex and may depend on each particular domain’s property.

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“…For instance, peptides can be grafted to bioactive glasses using dopamine as a coupling agent, to get antifouling surfaces, while the peptide-surface interactions can be due to the van der Waals forces, such as the hydrogen bond, electrostatic attraction, hydrophobic effect, etc. [18,19].…”

Section: Introductionmentioning

confidence: 99%

Synthesis, Structure–Property Evaluation and Biological Assessment of Supramolecular Assemblies of Bioactive Glass with Glycyrrhizic Acid and Its Monoammonium Salt

Matchanov

Esanov²,

Renkawitz

et al. 2022

Materials

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Medical nutrients obtained from plants have been used in traditional medicine since ancient times, owning to the protective and therapeutic properties of plant extracts and products. Glycyrrhizic acid is one of those that, apart from its therapeutic effect, may contribute to stronger bones, inhibiting bone resorption and improving the bone structure and biomechanical strength. In the present study, we investigated the effect of a bioactive glass (BG) addition to the structure–property relationships of supramolecular assemblies formed by glycyrrhizic acid (GA) and its monoammonium salt (MSGA). FTIR spectra of supramolecular assemblies evidenced an interaction between BG components and hydroxyl groups of MSGA and GA. Moreover, it was revealed that BG components may interact and bond to the carboxyl groups of MSGA. In order to assess their biological effects, BG, MSGA, and their supramolecular assemblies were introduced to a culture of human bone-marrow-derived mesenchymal stromal cells (BMSCs). Both the BG and MSGA had positive influence on BMSC growth, viability, and osteogenic differentiation—these positive effects were most pronounced when BG1d-BG and MSGA were introduced together into cell culture in the form of MSGA:BG assemblies. In conclusion, MSGA:BG assemblies revealed a promising potential as a candidate material intended for application in bone defect reconstruction and bone tissue engineering approaches.

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Ultrahigh Adhesion Force Between Silica-Binding Peptide SB7 and Glass Substrate Studied by Single-Molecule Force Spectroscopy and Molecular Dynamic Simulation

Cited by 21 publications

References 44 publications

Pathogen-Host Adhesion between SARS-CoV-2 Spike Proteins from Different Variants and Human ACE2 Probed at Single-Molecule and Single-Cell Levels

Pathogen-Host Adhesion between SARS-CoV-2 Spike Proteins from Different Variants and Human ACE2 Probed at Single-Molecule and Single-Cell Levels

Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin

Synthesis, Structure–Property Evaluation and Biological Assessment of Supramolecular Assemblies of Bioactive Glass with Glycyrrhizic Acid and Its Monoammonium Salt

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