Binding Potency of Peptide Fragments of Type 1 Collagen Cross-Linked N Telopeptide Measured by an Enzyme-Linked Immunosorbant Assay

Feng-Di   T.   Lung; Chiu-Heng      Chen; Heuy-Yi      Chen; Chien-Chung      Liou; Yen-Meng      Liou

Abstract

Osteoporosis represents a major healthcare problem affecting elderly person. Urinary level of the crosslinked N-telopeptide of type I collagen is a sensitive marker of bone resorption. Ten overlapping peptides covering the N-telopeptide of alpha-2 type I collagen were synthesized, purified, and assayed for their relative binding response to anti-type I collagen cross-linked N-telopeptide (NTX) antibody by using a competitive-inhibition enzyme-linked immunosorbent assay (ELISA). Peptides 1, 2, and 3, containing the N-terminal sequence of Ntelopeptide, showed higher binding potency than peptides 4-10, suggesting that these peptides may contain binding sites for anti-NTX antibodies, and can serve as the lead for further preparation of their antibodies in order to develop novel bioassays for monitoring the bone loss in humans.

Keywords: osteoporosis, cross-linked N-telopeptide, type I collagen, synthetic overlapping peptides, solid phase, peptide synthesis, high performance liquid chromatography, enzyme-linked immunosorbent assay