scholarly journals Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri

Antibiotics ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 895
Author(s):  
Yaxian Lin ◽  
Siyan Liu ◽  
Xinping Xi ◽  
Chengbang Ma ◽  
Lei Wang ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antibiotic Resistance ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Resistant Bacteria ◽  
Skin Secretion ◽  
Structure Activity ◽  
Active Fragments ◽  
Net Charges ◽  
Relationship Of

Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were designed to explore the structure–activity relationship and enhance its activity. In general, the Rana box is not an indispensable motif for the bioactivity of Brevinin-2GUb, and the first to the 19th amino acids at the N-terminal end are active fragments, such that shortening the peptide while maintaining its bioactivity is a promising strategy for the optimisation of peptides. Keeping a complete hydrophobic face and increasing the net charges are key factors for antimicrobial activity. With the increase of cationic charges, α-helical proportion, and amphipathicity, the activity of t-Brevinin-2GUb-6K (tB2U-6K), in combatting bacteria, drastically improved, especially against Gram-negative bacteria, and the peptide attained the capacity to kill clinical isolates and fungi as well, which made it possible to address some aspects of antibiotic resistance. Thus, peptide tB2U-6K, with potent antimicrobial activity against antibiotic-resistant bacteria, the capacity to inhibit the growth of biofilm, and low toxicity against normal cells, is of value to be further developed into an antimicrobial agent.

SYNTHESIS AND STRUCTURE-ACTIVITY RELATIONSHIP OF NEW BENZIMIDAZOLE DERIVATIVES AS ANTIMICROBIAL AGENTS

INDIAN DRUGS ◽  
2012 ◽  
Vol 49 (03) ◽  
pp. 25-29
Author(s):  
S. G Jadhav ◽  
◽  
S. R. Pattan
Keyword(s):  
Antimicrobial Activity ◽  
Spectral Data ◽  
Antimicrobial Agents ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Benzimidazole Derivatives ◽  
Structure Activity ◽  
Relationship Of

A new series of substituted benzimidazole derivatives were synthesized and the structures of these compounds were established on the basis of spectral data. The title compounds were evaluated for antimicrobial activity. Some of these compounds have shown excellent antimicrobial activity.

scholarly journals Structure–Activity Relationship and Molecular Docking of a Kunitz-Like Trypsin Inhibitor, Kunitzin-AH, from the Skin Secretion of Amolops hainanensis

Pharmaceutics ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 966
Author(s):  
Yuqing Chen ◽  
Xinping Xi ◽  
Chengbang Ma ◽  
Mei Zhou ◽  
Xiaoling Chen ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Inhibitory Activity ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Skin Secretion ◽  
Site Mutation ◽  
Structure Activity ◽  
Hydrophilic Residues ◽  
Inhibitory Drug ◽  
Relationship Of

Kunitz-like trypsin inhibitors are one of the most noteworthy research objects owing to their significance in pharmacological studies, including anticarcinogenic activity, obesity regulation and anticoagulation. In the current study, a novel Kunitz-like trypsin inhibitor, Kunitzin-AH, was isolated from the skin secretion of Amolops hainanensis. The novel peptide displayed a modest trypsin inhibitory activity with the inhibitor constant (Ki) value of 1.18 ± 0.08 µM without inducing damage to healthy horse erythrocytes. Then, a series of shortened variants of Kunitzin-AH were designed by truncating a peptide loop and site mutation inside the loop to illustrate the structure–activity relationship of the trypsin inhibition function. Among the variants, a significant decrease was observed for the Cys-Cys loop domain, while the extension of an Arg at N-terminus (RCKAAFC) retained the inhibitory activity, indicating that the -RCK-motif is essential in forming the reactive domain for exerting the inhibitory activity. Furthermore, substitutions of Ala by hydrophobic or hydrophilic residues decreased the activity, indicating suitable steric hindrance provides convenience for the combination of trypsin. Additionally, the conformational simulation of the analogues processed with Chimera and Gromacs and further combination simulations between the peptides and trypsin conducted with HDOCK offered a potential opportunity for the natural trypsin inhibitory drug design. The truncated sequence, AH-798, may be a good replacement for the full-length peptide, and can be optimized via cyclization for further study.

scholarly journals Modification and Targeted Design of N-Terminal Truncates Derived from Brevinin with Improved Therapeutic Efficacy

Biology ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 209
Author(s):  
Haoyang He ◽  
Yuqing Chen ◽  
Zhuming Ye ◽  
Xiaoling Chen ◽  
Chengbang Ma ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Immune Regulation ◽  
Structure Activity Relationship ◽  
Innate Immune ◽  
Activity Relationship ◽  
Potential Toxicity ◽  
Structure Activity ◽  
Starting Point ◽  
Haemolytic Assay ◽  
Relationship Of

Antimicrobial peptides (AMPs) are a class of molecules that play an essential role in innate immune regulation. The Brevinin-1 family are AMPs that show strong pharmacological and antimicrobial potential. A novel peptide, B1A, was designed based on the primary structure of brevinin-1PLb and brevinin-1PLc. Subsequently, a synthesised replicate was subjected to a series of bioassays and was found to display antimicrobial activity. However, it also displayed high levels of haemolysis in a horse red blood cell haemolytic assay, suggesting potential toxicity. Therefore, we rationally designed a number of B1A analogues with aim of retaining antimicrobial activity, lowering toxicity, and to explore the structure–activity relationship of its N-terminus. B1A and its analogues still retained the “Rana Box” and the FLP-motif, which is a feature of this subfamily. However, the introduction of Lys and Trp residues into the peptide sequences revealed that antimicrobial activity of these analogues remained unchanged once the hydrophobicity and the charge reached the threshold. Hence, the idea that the hydrophobicity saturation in different situations is related to antimicrobial activity can be understood via the structure–activity relationship. Meanwhile, it could also be the starting point for the generation of peptides with specific antimicrobial activity.

scholarly journals Structure-activity relationship of HP (2–20) analog peptide: Enhanced antimicrobial activity by N-terminal random coil region deletion

Biopolymers ◽  
2007 ◽  
Vol 88 (2) ◽  
pp. 199-207 ◽  
Author(s):  
Yoonkyung Park ◽  
Seong-Cheol Park ◽  
Hae-Kyun Park ◽  
Song Yub Shin ◽  
Yangmee Kim ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Structure Activity Relationship ◽  
Random Coil ◽  
Activity Relationship ◽  
Structure Activity ◽  
Analog Peptide ◽  
Relationship Of

scholarly journals Structure-Activity Relationship of Benzophenanthridine Alkaloids from Zanthoxylum rhoifolium Having Antimicrobial Activity

PLoS ONE ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. e97000 ◽  
Author(s):  
Luciana de C. Tavares ◽  
Graciane Zanon ◽  
Andréia D. Weber ◽  
Alexandre T. Neto ◽  
Clarice P. Mostardeiro ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Benzophenanthridine Alkaloids ◽  
Structure Activity ◽  
Relationship Of

Structure-activity relationship of (-) mammea A/BB derivatives against Leishmania amazonensis

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
MA Brenzan ◽  
CV Nakamura ◽  
BPD Filho ◽  
T Ueda-Nakamura ◽  
MCM Young ◽  
...  
Keyword(s):  
Structure Activity Relationship ◽  
Leishmania Amazonensis ◽  
Activity Relationship ◽  
Structure Activity ◽  
Relationship Of
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