TY - JOUR
T1 - Peptide Solubility Limits
T2 - Backbone and Side-Chain Interactions
AU - Sarma, Rahul
AU - Wong, Ka Yiu
AU - Lynch, Gillian C.
AU - Pettitt, B. Montgomery
N1 - Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/4/5
Y1 - 2018/4/5
N2 - We calculate the solubility limit of pentapeptides in water by simulating the phase separation in an oversaturated aqueous solution. The solubility limit order followed by our model peptides (GGRGG > GGDGG > GGGGG > GGVGG > GGQGG > GGNGG > GGFGG) is found to be the same as that reported for amino acid monomers from experiment (R > D > G > V > Q > N > F). Investigation of dynamical properties of peptides shows that the higher the solubility of a peptide is, the lower the time spent by the peptide in the aggregated cluster is. We also demonstrate that fluctuations in conformation and hydration number of peptide in monomeric form are correlated with the solubility of the peptide. We considered energetic mechanisms and dynamical properties of interbackbone CO-CO and CO···HN interactions. Our results confirm that CO-CO interactions more than the interbackbone H-bonds are important in peptide self-assembly and association. Further, we find that the stability of H-bonded peptide pairs arises mainly from coexisting CO-CO and CO···HN interactions.
AB - We calculate the solubility limit of pentapeptides in water by simulating the phase separation in an oversaturated aqueous solution. The solubility limit order followed by our model peptides (GGRGG > GGDGG > GGGGG > GGVGG > GGQGG > GGNGG > GGFGG) is found to be the same as that reported for amino acid monomers from experiment (R > D > G > V > Q > N > F). Investigation of dynamical properties of peptides shows that the higher the solubility of a peptide is, the lower the time spent by the peptide in the aggregated cluster is. We also demonstrate that fluctuations in conformation and hydration number of peptide in monomeric form are correlated with the solubility of the peptide. We considered energetic mechanisms and dynamical properties of interbackbone CO-CO and CO···HN interactions. Our results confirm that CO-CO interactions more than the interbackbone H-bonds are important in peptide self-assembly and association. Further, we find that the stability of H-bonded peptide pairs arises mainly from coexisting CO-CO and CO···HN interactions.
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U2 - 10.1021/acs.jpcb.7b10734
DO - 10.1021/acs.jpcb.7b10734
M3 - Article
C2 - 29384681
AN - SCOPUS:85045046087
SN - 1520-6106
VL - 122
SP - 3528
EP - 3539
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 13
ER -