Evidence that L1AD3, an apoptosis-inducing cyclic peptide, binds a leukemic T-cell membrane protein receptor.

Abstract:

:Human leukemic T-lymphocytes undergo extensive and rapid apoptosis in the presence of L1AD3, a small cyclic peptide derivative of cobra cardiotoxin. The first step in this process involves its binding to membranes of susceptible cells. By the use of a biotin "handle" synthetically incorporated at the N-terminus of L1AD3, we show that binding is saturable and selective: normal human peripheral blood lymphocytes do not bind this peptide. Fluorescence resonance energy transfer experiments indicate that the binding sites are separated by at least 55 A. Loss of binding occurs if membrane proteins are enzymatically degraded, suggesting that L1AD3's target is a cell-membrane surface protein receptor. Finally, crosslinking of cyclic BTNL1AD3 peptide to a leukemic T-cell membrane surface receptor, as examined using a biotin-avidin blot, indicated a molecular weight of approximately 34,400.

journal_name

Arch Biochem Biophys

authors

Smith CA,Hinman CL

doi

10.1016/j.abb.2004.08.010

subject

Has Abstract

pub_date

2004-12-01 00:00:00

pages

88-101

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(04)00463-1

journal_volume

432

pub_type

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