Volume 4, Issue 5 pp. 917-924
Research Article

Two New Protease-Inhibiting Glycosphingolipids from Buddleja crispa

Ijaz Ahmad

Ijaz Ahmad

H. E. J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan, (phone: +92-21-4824926)

Search for more papers by this author
Itrat Anis

Itrat Anis

H. E. J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan, (phone: +92-21-4824926)

Search for more papers by this author
Itrat Fatima

Itrat Fatima

H. E. J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan, (phone: +92-21-4824926)

Search for more papers by this author
Abdul Malik

Abdul Malik

H. E. J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan, (phone: +92-21-4824926)

Search for more papers by this author
Shafiullah Khan

Shafiullah Khan

Pharmaceutical Research Centre, PCSIR, Laboratories Complex Karachi, Karachi-75280, Pakistan

Search for more papers by this author
Nighat Afza

Nighat Afza

Pharmaceutical Research Centre, PCSIR, Laboratories Complex Karachi, Karachi-75280, Pakistan

Search for more papers by this author
Rasool Bakhsh Tareen

Rasool Bakhsh Tareen

Department of Botany, Baluchistan University, Saryab Road, Quetta, Pakistan

Search for more papers by this author
Muhammad Arif Lodhi

Muhammad Arif Lodhi

H. E. J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan, (phone: +92-21-4824926)

Search for more papers by this author
M. Iqbal Choudhary

M. Iqbal Choudhary

H. E. J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan, (phone: +92-21-4824926)

Search for more papers by this author
First published: 18 May 2007
Citations: 5

Abstract

Crispins A (1) and B (2), two new glycosphingolipids, were isolated from the whole plant Buddleja crispa, along with three known compounds: α-amyrin, linoleic acid, and stigmasterol. Their structures were elucidated by chemical and spectroscopic techniques. Both 1 and 2 showed significant inhibitory activity against α-chymotrypsin in a concentration-dependent manner.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.