Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus

Gao, Bin; Xu, Jia; Rodrı́guez, Marı́a del Carmen; Lanz‐Mendoza, Humberto; Hernández‐Rivas, Rosaura; Du, Weihong; Zhu, Shunyi

doi:10.1016/j.biochi.2010.01.011

Cited by 84 publications

(58 citation statements)

References 51 publications

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“…This intermediate was found to be involved in a rate-limiting step of the folding reaction. CD and NMR studies of two antimalarial peptides have also been shown to promote α-helical conformations in TFE [12]. Comparison of folding free energy of a of poly-alanine peptide sequence in different alcohols showed that TFE stabilizes α-helical conformation better than ethanol, methanol, and pure water, as shown by CD and UV resonance Raman spectroscopy.…”

Section: Introductionmentioning

confidence: 94%

Environmental polarity induces conformational transitions in a helical peptide sequence from bacteriophage T4 lysozyme and its tandem duplicate: a molecular dynamics simulation study

Kaur

Sasidhar

2015

J Mol Model

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Our recent molecular dynamics (MD) simulation of an insertion/duplication mutant 'L20' of bacteriophage T4 lysozyme demonstrated a solvent induced α→β transition in a loosely held duplicate helical region, while α-helical conformation in the parent region was relatively stabilized by its tertiary interactions with the neighboring residues. The solution NMR of the parent helical sequence, sans its protein context, showed no inherent tendency to adopt a particular secondary structure in pure water but showed α-helical propensity in TFE/water and SDS micelles. In this study we investigate the conformational preference of the 'parent' and 'duplicate' sequences, sans the protein context, in pure water and an apolar TFE/water solution. Apolar TFE/water solution is a model for non-polar protein context. We performed MD simulations of the two peptides, in explicit water and 80% (v/v) TFE/water, using GROMOS 53a6 force field, at 300 K and 1 bar (under NPT conditions). We show that in TFE/water mixture, salt bridges are stabilized by apolar TFE molecules and main chain-main chain hydrogen bonds promote the α-helical conformation, particularly in the duplicate peptide. Solvent exposure, in pure water, resulted in an α→β transition to form a triple stranded β-sheet structure in the 'duplicate' sequence, with a rare psi-loop topology, while a mixture of turn/bend conformations were adopted by the 'parent' sequence. Thus the differences in conformational preference of the parent and duplicate sequence sans protein context, in pure water and TFE/water, implicate the importance of the environment polarity in dictating the peptide conformation. Mechanism of folding of the observed psi-loop in the duplicate sequence gives insights into folding of this rare β-sheet topology.

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Section: Introductionmentioning

confidence: 94%

Environmental polarity induces conformational transitions in a helical peptide sequence from bacteriophage T4 lysozyme and its tandem duplicate: a molecular dynamics simulation study

Kaur

Sasidhar

2015

J Mol Model

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“…The structure of IsCT [59] in the space-filling model is presented in Figure 1G. The structure of meucin-24 is another typical amphipathic helix [60]. (Structures of other helical peptides were not deposited into the PDB).…”

Section: Three-dimensional Structurementioning

confidence: 99%

Insights into Antimicrobial Peptides from Spiders and Scorpions

Wang¹,

Wang

2016

PPL

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The venoms of spiders and scorpions contain a variety of chemical compounds. Antimicrobial peptides (AMPs) from these organisms were first discovered in the 1990s. As of May 2015, there were 42 spider’s and 63 scorpion’s AMPs in the Antimicrobial Peptide Database (http://aps.unmc.edu/AP). These peptides have demonstrated broad or narrow-spectrum activities against bacteria, fungi, viruses, and parasites. In addition, they can be toxic to cancer cells, insects and erythrocytes. To provide insight into such an activity spectrum, this article discusses the discovery, classification, structure and activity relationships, bioinformatics analysis, and potential applications of spider and scorpion AMPs. Our analysis reveals that, in the case of linear peptides, spiders use both glycine-rich and helical peptide models for defense, whereas scorpions use two distinct helical peptide models with different amino acid compositions to exert the observed antimicrobial activities and hemolytic toxicity. Our structural bioinformatics study improves the knowledge in the field and can be used to design more selective peptides to combat tumors, parasites, and viruses.

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“…32 and 33). More promising candidates for therapeutic applications are NDPs with very low or non-recorded cytolytic activity against mammalian cells, such as Meucin-24 and Meucin-25, two peptides from Mesobuthus eupeus venom with plasmodicidal activity, 34 BmKbpp, a multi-functional AMP from Mesobuthus martensii, 35 and the antibacterial VmCT2 from Vaejovis mexicanus. 36 Moreover, some scorpionvenom AMPs can also act synergistically with conventional antibiotics.…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%