structure activity
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2022 ◽  
Vol 146 ◽  
pp. 127-145
Tuyelee Das ◽  
Suchismita Chatterjee Saha ◽  
Kumari Sunita ◽  
Madhumita Majumder ◽  
Mimosa Ghorai ◽  

Nano Today ◽  
2022 ◽  
Vol 42 ◽  
pp. 101354
Cong Li ◽  
Xiaoyun Qin ◽  
Zhenghao Zhang ◽  
Yujia Lv ◽  
Shengwei Zhang ◽  

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 561
Prapenpuksiri Rungsa ◽  
Steve Peigneur ◽  
Nisachon Jangpromma ◽  
Sompong Klaynongsruang ◽  
Jan Tytgat ◽  

Antimicrobial peptides are an important class of therapeutic agent used against a wide range of pathogens such as Gram-negative and Gram-positive bacteria, fungi, and viruses. Mastoparan (MpVT) is an α-helix and amphipathic tetradecapeptide obtained from Vespa tropica venom. This peptide exhibits antibacterial activity. In this work, we investigate the effect of amino acid substitutions and deletion of the first three C-terminal residues on the structure–activity relationship. In this in silico study, the predicted structure of MpVT and its analog have characteristic features of linear cationic peptides rich in hydrophobic and basic amino acids without disulfide bonds. The secondary structure and the biological activity of six designed analogs are studied. The biological activity assays show that the substitution of phenylalanine (MpVT1) results in a higher antibacterial activity than that of MpVT without increasing toxicity. The analogs with the first three deleted C-terminal residues showed decreased antibacterial and hemolytic activity. The CD (circular dichroism) spectra of these peptides show a high content α-helical conformation in the presence of 40% 2,2,2- trifluoroethanol (TFE). In conclusion, the first three C-terminal deletions reduced the length of the α-helix, explaining the decreased biological activity. MpVTs show that the hemolytic activity of mastoparan is correlated to mean hydrophobicity and mean hydrophobic moment. The position and spatial arrangement of specific hydrophobic residues on the non-polar face of α-helical AMPs may be crucial for the interaction of AMPs with cell membranes.

Cancers ◽  
2022 ◽  
Vol 14 (2) ◽  
pp. 346
Meilan Hu ◽  
Fule He ◽  
Erik W. Thompson ◽  
Kostya (Ken) Ostrikov ◽  
Xiaofeng Dai

Acetylation, a reversible epigenetic process, is implicated in many critical cellular regulatory systems including transcriptional regulation, protein structure, activity, stability, and localization. Lysine acetylation is the most prevalent and intensively investigated among the diverse acetylation forms. Owing to the intrinsic connections of acetylation with cell metabolism, acetylation has been associated with metabolic disorders including cancers. Yet, relatively little has been reported on the features of acetylation against the cancer hallmarks, even though this knowledge may help identify appropriate therapeutic strategies or combinatorial modalities for the effective treatment and resolution of malignancies. By examining the available data related to the efficacy of lysine acetylation against tumor cells and elaborating the primary cancer hallmarks and the associated mechanisms to target the specific hallmarks, this review identifies the intrinsic connections between lysine acetylation and cancer hallmarks and proposes novel modalities that can be combined with HDAC inhibitors for cancer treatment with higher efficacy and minimum adverse effects.

C. Alimenti ◽  
F. Buonanno ◽  
G. Di Giuseppe ◽  
G. Guella ◽  
P. Luporini ◽  

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