April 2001 Meeting Announcement, Delaware Valley Mass Spectrometry Discussion Group
- Topic: "A Study of Peptide-peptide Interaction Using various Mass Spectrometric Techniques"
- Speaker: Amina Woods, NIDA/IRP
- Date: Monday, April 9, 2001. 7:00 PM
- Time: Social Hour: 7:00 PM.
Talk: 7:30 PM.
- Place: Merck, West Point, 37 Auditorium
- Abstract: Matrix assisted laser desorption/ionization (MALDI) mass spectrometry has been used to study peptide-peptide interactions with 6-aza-2-thiothymine (ATT) matrix (at pH 5.4). However the interaction was disrupted with a more acidic matrix, a-cyano-4-hydroxycinnamic acid (pH 2.0) [A.S. Woods and M.A. Huestis, A Study of Peptide Peptide Interaction by MALDI JASMS 12, 88-96 (2001)]. Several basic peptides, including the opioid peptide dynorphin 1-7 (D1-7: YGGFLRR), and RKRARKE have been shown to bind to acidic peptides, such as mini-Gastrin I (LEEEEEAYGWMDF-NH2). The adjacent basic residues (Arg6 - Arg7 or RKR), allow non-covalent interaction with peptides that contain two to five adjacent acidic residues (Asp or Glu). These complexes were also investigated using MALDI-Ion Mobility (IM)-MALDI TOF, ESI-TOF mass spectrometry and AP MALDI/Ion trap.
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