Nowadays α-amylase is widely used in various fields. Therefore, in this study, the effects of neutral (T), negatively charged (T) and positively charged (T) peptides on α-amylase activity were investigated by means of an applied protein electric field, and spectroscopy and molecular dynamics were employed to investigate this mechanism. It was found that the nature of the charge of the peptides had a strong influence on α-amylase activity, with T and T increasing and decreasing α-amylase activity, respectively, whereas T had no effect on enzyme activity. Fluorescence spectroscopy and circular dichroism results indicated that the charged peptides changed the conformation of α-amylase. Meanwhile, the molecular dynamics results showed that the charged peptides changed the distribution of the surface charge of α-amylase mainly through electrostatic force, which not only changed the conformation of the enzyme, but also altered the microenvironment of the enzyme active centre, which caused α-amylase to become compact or loose to affect the enzyme activity.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bioorg.2024.107972 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Synergistic Enhancement of Ferroptosis via Mitochondrial Accumulation and Photodynamic-Controlled Release of an Organogold(I) Cluster Prodrug.
J Am Chem Soc
January 2025
Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, P. R. China.
Effective delivery and controlled release of metallo-prodrugs with sustained activation and rapid response feed the needs of precise medicine in metal chemotherapeutics. However, gold-based anticancer drugs often suffer from detoxification binding and extracellular transfer by sulfur-containing peptides. To address this challenge, we integrate a thiol-activated prodrug strategy of newly prepared hypercoordinated carbon-centered gold(I) clusters (HCGCs) with their photosensitization character to augment the mitochondrial release of Au(I) in tumors.
View Article and Find Full Text PDFUltrasound assisted complexation of soybean peptide aggregates and soluble soybean polysaccharide: pH optimization, structure characterization, and emulsifying behavior.
Food Res Int
February 2025
Engineering and Technology Center for Grain Processing of Shandong Province, Key Laboratory of Food Processing Technology and Quality Control in Shandong Province, College of Food Science and Engineering, Shandong Agricultural University, 61 Daizong Avenue, Tai'an 271018, China. Electronic address:
This study aims to enhance the emulsifying properties of soybean peptide aggregates (SPA) by preparing SPA-soluble soybean polysaccharide (SSPS) composite particles at the assistance of ultrasound technique. The optimal pH for SPA and SSPS complexation was determined by measuring the charge and particle size of the composites. The effects of ultrasound power and duration on the physicochemical properties of the composite particles were assessed through measurements of particle size, zeta potential, contact angle, FTIR, and SEM.
View Article and Find Full Text PDFBioorthogonal reaction-mediated photosensitizer-peptide conjugate anchoring on cell membranes for enhanced photodynamic therapy.
Biomater Sci
January 2025
School of Engineering, Westlake University, Hangzhou, Zhejiang 310023, China.
Photodynamic therapy (PDT), utilizing a photosensitizer (PS) to induce tumor cell death, is an effective modality for cancer treatment. PS-peptide conjugates have recently demonstrated remarkable antitumor potential in preclinical trials. However, the limited cell membrane binding affinity and rapid systemic clearance have hindered their transition to clinical applications.
View Article and Find Full Text PDF[Vacuum ultraviolet laser dissociation and proteomic analysis of halogenated peptides].
Se Pu
February 2025
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Chemical modifications are widely used in research fields such as quantitative proteomics and interaction analyses. Chemical-modification targets can be roughly divided into four categories, including those that integrate isotope labels for quantification purposes, probe the structures of proteins through covalent labeling or cross-linking, incorporate labels to improve the ionization or dissociation of characteristic peptides in complex mixtures, and affinity-enrich various poorly abundant protein translational modifications (PTMs). A chemical modification reaction needs to be simple and efficient for use in proteomics analysis, and should be performed without any complicated process for preparing the labeling reagent.
View Article and Find Full Text PDFAntimicrobial peptide glatiramer acetate targets Pseudomonas aeruginosa lipopolysaccharides to breach membranes without altering lipopolysaccharide modification.
NPJ Antimicrob Resist
February 2024
National Heart and Lung Institute, Imperial College London, London, UK.
Antimicrobial peptides (AMPs) are key components of innate immunity across all domains of life. Natural and synthetic AMPs are receiving renewed attention in efforts to combat the antimicrobial resistance (AMR) crisis and the loss of antibiotic efficacy. The gram-negative pathogen Pseudomonas aeruginosa is one of the most concerning infecting bacteria in AMR, particularly in people with cystic fibrosis (CF) where respiratory infections are difficult to eradicate and associated with increased morbidity and mortality.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!