Bioactive Peptides

    The following biologically relevant peptides were studied (structure and/or hydration):

• Bradykinin (plasma polypeptide)
• molecule shape [1]
• the question of salt bridges [1]
• hydration [2]
• LHRH (hypothalamic hormone) [2]
• structure
• hydration
• Neurotensin (gastrointestinal hormone)
  • hydration [2]
• Oxytocin (pituitary hormone) [3]
  • affinity for divalent metal ions
  • structure (see our peptide folding page)
  • hydration
• Amyloid β-peptide (extracellular protein involved in Alzheimer's disease) [4]
  • structure and early stages of aggregation

References and comments:

1. "Gas-phase conformation of biological molecules: Bradykinin" T. Wyttenbach, G. von Helden, M. T. Bowers J. Am. Chem. Soc. 1996, 118, 8355-8364
   
   
2. Hydration of bradykinin and LHRH was studied by experiment and molecular modeling. Results are briefly discussed in the context of zwitterions on our zwitterion web page. Experimental hydration results on bradykinin, LHRH, and neurotensin and some aspects of the modeling results on bradykinin and LHRH are covered in the following two publications.
   
   
   • "Sequential hydration of small protonated peptides" D. Liu, T. Wyttenbach, P. E. Barran, M. T. Bowers J. Am. Chem. Soc. 2003, 125, 8458-8464
     
     
   • "Hydration of small peptides" T. Wyttenbach, D. Liu, M. T. Bowers Int. J. Mass Spectrom. 2005, 240, 221-232
   
   
3. "Oxytocin-receptor binding: Why divalent metals are essential" D. Liu, A. B. Seuthe, O. T. Ehrler, X. Zhang, T. Wyttenbach, J. F. Hsu, M. T. Bowers J. Am. Chem. Soc. 2005, 127, 2024-2025
   
   
4. "Amyloid β-protein: Monomer structure and early aggregation states of Aβ42 and its Pro¹⁹ alloform" S. L. Bernstein, T. Wyttenbach, A. Baumketner, J.-E. Shea, G. Bitan, D. B. Teplow, M. T. Bowers J. Am. Chem. Soc. 2005, 127, 2075-2084