Influence of solvents on conformation of dehydropeptides

Jewgiński, Michał; Latajka, Rafał; Krężel, Artur; Haremza, Kinga; Makowski, Maciej; Kafarski, Paweł

doi:10.1016/j.molstruc.2012.08.042

Cited by 18 publications

(6 citation statements)

References 59 publications

(75 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As could be seen from our previous investigations, an increase in solvent polarity promotes more ordered conformations of hexapeptides containing two dehydrophenylalanine residues [38]. On the other hand, Inai and co-workers showed that in the case of dehydropeptides containing only one chiral L-residue in the N-terminal position of the peptide a left-handed helical conformation is adopted regardless of the solvent polarity [39], but when a chiral residue occupied the second position of the peptide, the screw sense of the helix depends on the type of solvent [40].…”

Section: Resultsmentioning

confidence: 76%

Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Jewgiński¹,

Krzciuk-Gula²,

Makowski³

et al. 2014

Beilstein J. Org. Chem.

Self Cite

View full text Add to dashboard Cite

SummaryStructural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.

show abstract

Section: Resultsmentioning

confidence: 76%

Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Jewgiński¹,

Krzciuk-Gula²,

Makowski³

et al. 2014

Beilstein J. Org. Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Additionally, tripeptide 161 and tetrapeptide 162 were found to exhibit more ordered conformations as the polarity of the solvent was increased. 142 Whereas the conformational preferences and turn-inducing properties of Z-DPhe are well-established, much less is known about E-DPhe. Using a combination of NMR, IR, and DFT techniquies, Broda and co-workers compared the conformations of N 0 ,N 0 -dimethylamides 164 and 165, which contain E-and Z-DPhe, respectively (Fig.…”

Section: Peptides Containing Trisubstituted Ab-dehydroamino Acidsmentioning

confidence: 99%

Bulky α,β-dehydroamino acids: their occurrence in nature, synthesis, and applications

Jiang

Castle

2015

Tetrahedron

View full text Add to dashboard Cite

“…Thus for peptides with low helical propensity 30-50 % TFE concentration is required to maximally stabilize their helical conformation while that for peptides with smaller helical propensity is 80 %. Also, it has been shown that the effect of solvent polarity influences the peptide conformations based on its chain length, as suggested by N M R , C D a n d m o l e c u l a r m o d e l i n g s t u d i e s o f dehydropeptides containing (Z)-dehydrophenylalanine [22]. Apart from this it has been suggested that the helix formation propensity in TFE depends on its amino acid sequence [23].…”

Section: Introductionmentioning

confidence: 95%

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

View full text Add to dashboard Cite

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.

show abstract

Influence of solvents on conformation of dehydropeptides

Cited by 18 publications

References 59 publications

Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Bulky α,β-dehydroamino acids: their occurrence in nature, synthesis, and applications

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

Contact Info

Product

Resources

About