Abstract
In this study, mechanistic insights into the hydrolysis of an extremely stable tertiary peptide bond (Ser-Pro) in the Ser-Pro-Phe sequence by an artificial enzyme, metal (Pd2+, Co2+, or Zn 2+)-β-cyclodextrin (CD) complex, have been provided. In particular, the exact reaction mechanism, the location of CD (number of -CH 2 groups downstream from the metal center), conformation of CD (primary or secondary rim of CD facing the substrate), the number of CD (one or two), and the optimum metal ion (Pd2+, Co2+, or Zn 2+) have been suggested using a state-of-the-art hybrid quantum mechanics/molecular mechanics (QM/MM: B3LYP/Amber) approach. The QM/MM calculations suggest that the internal delivery mechanism is the most energetically feasible for the peptide hydrolysis. The inclusion of a CD ring at two CH2 groups downstream from the metal center can provide 3 × 105 times acceleration in the activity, while the replacement of Pd2+ with Co2+ enhances the rate activity another 3.7 × 104 times.
| Original language | English |
|---|---|
| Pages (from-to) | 4106-4114 |
| Number of pages | 9 |
| Journal | Journal of Physical Chemistry B |
| Volume | 118 |
| Issue number | 15 |
| DOIs | |
| State | Published - Apr 17 2014 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Materials Chemistry
- Surfaces, Coatings and Films
Cite this
Mechanistic insights into metal (Pd2+, Co2+, and Zn2+)-β-cyclodextrin catalyzed peptide hydrolysis : A QM/MM approach. / Zhang, Tingting; Zhu, Xiaoxia; Prabhakar, Rajeev.
In: Journal of Physical Chemistry B, Vol. 118, No. 15, 17.04.2014, p. 4106-4114.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Mechanistic insights into metal (Pd2+, Co2+, and Zn2+)-β-cyclodextrin catalyzed peptide hydrolysis
T2 - A QM/MM approach
AU - Zhang, Tingting
AU - Zhu, Xiaoxia
AU - Prabhakar, Rajeev
PY - 2014/4/17
Y1 - 2014/4/17
N2 - In this study, mechanistic insights into the hydrolysis of an extremely stable tertiary peptide bond (Ser-Pro) in the Ser-Pro-Phe sequence by an artificial enzyme, metal (Pd2+, Co2+, or Zn 2+)-β-cyclodextrin (CD) complex, have been provided. In particular, the exact reaction mechanism, the location of CD (number of -CH 2 groups downstream from the metal center), conformation of CD (primary or secondary rim of CD facing the substrate), the number of CD (one or two), and the optimum metal ion (Pd2+, Co2+, or Zn 2+) have been suggested using a state-of-the-art hybrid quantum mechanics/molecular mechanics (QM/MM: B3LYP/Amber) approach. The QM/MM calculations suggest that the internal delivery mechanism is the most energetically feasible for the peptide hydrolysis. The inclusion of a CD ring at two CH2 groups downstream from the metal center can provide 3 × 105 times acceleration in the activity, while the replacement of Pd2+ with Co2+ enhances the rate activity another 3.7 × 104 times.
AB - In this study, mechanistic insights into the hydrolysis of an extremely stable tertiary peptide bond (Ser-Pro) in the Ser-Pro-Phe sequence by an artificial enzyme, metal (Pd2+, Co2+, or Zn 2+)-β-cyclodextrin (CD) complex, have been provided. In particular, the exact reaction mechanism, the location of CD (number of -CH 2 groups downstream from the metal center), conformation of CD (primary or secondary rim of CD facing the substrate), the number of CD (one or two), and the optimum metal ion (Pd2+, Co2+, or Zn 2+) have been suggested using a state-of-the-art hybrid quantum mechanics/molecular mechanics (QM/MM: B3LYP/Amber) approach. The QM/MM calculations suggest that the internal delivery mechanism is the most energetically feasible for the peptide hydrolysis. The inclusion of a CD ring at two CH2 groups downstream from the metal center can provide 3 × 105 times acceleration in the activity, while the replacement of Pd2+ with Co2+ enhances the rate activity another 3.7 × 104 times.
UR - http://www.scopus.com/inward/record.url?scp=84898984940&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84898984940&partnerID=8YFLogxK
U2 - 10.1021/jp502229s
DO - 10.1021/jp502229s
M3 - Article
C2 - 24713044
AN - SCOPUS:84898984940
VL - 118
SP - 4106
EP - 4114
JO - Journal of Physical Chemistry B Materials
JF - Journal of Physical Chemistry B Materials
SN - 1520-6106
IS - 15
ER -