------- Forwarded Message Follows -------
From: Self <UNIKKO/KANTORAA>
To: abrf@aecom.yu.edu
Subject: Peptide synthesis inquire
Cc: Hanri.Huttunen@helsinki.fi
Reply-to: Carmela.Kantor-Aaltonen@helsinki.fi
Date: Wed, 14 Jun 2000 15:45:36 EET DST
Hi,
We have synthesized (2 times) a 34 aminoacid long peptide, sequence:
KLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKK. In the first synthesis we had
problems in coupling Asp (according to the mass-analysis), and we
resynthesized the peptide using double couplings for both Asp:s,
used capping and Hmb-Ala (to avoid aspartamide formation). The
result was a peptide with the right mass, but it was totally inactive
in biological experiments. Edman degradation for the peptide gave the
right aminoacids until it reached the first Asp, where the sequencing
stopped. We assume thet there has occured a ring formation for the
Asp, and the ring has opened "in the wrong" (D,L) direction.
If you have any ideas concerning this particular synthesis, please
let me know. How to avoid the possible ring formation, which
seemed to be total 100% (!!!) according to the Edman degradation (we
couldnĄt get any sequence after K)
Thank You
Cami Kantor
----------------------------------------------------------------------
Carmela Kantor-Aaltonen
Division of Biochemistry
Department of Biosciences
P.O.Box 56 (Viikinkaari 5)
00014 University of Helsinki
Finland
tel. +358-9-19159035
fax. +358-9-19159068
Email: Carmela.Kantor-Aaltonen@Helsinki.fi
This archive was generated by hypermail 2b29 : Fri Jun 30 2000 - 07:51:55 EDT