Publication:
Efficient photocleavage of lysozyme by a new chiral probe

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Issued Date

2005

Resource Type

Review

File Type

application/pdf

ISSN

15701786

DOI

10.2174/1570178054640868

Other identifier(s)

2-s2.0-46149087568

Rights Holder(s)

Scopus

Bibliographic Citation

Letters in Organic Chemistry. Vol 2, No.6 (2005), p.554-558

Suggested Citation

Buranaprapuk A., Chaivisuthangkura P., Svasti J., Kumar C.V. Efficient photocleavage of lysozyme by a new chiral probe. Letters in Organic Chemistry. Vol 2, No.6 (2005), p.554-558. doi:10.2174/1570178054640868 Retrieved from: https://hdl.handle.net/20.500.14740/6080

Title

Efficient photocleavage of lysozyme by a new chiral probe

Author(s)

Buranaprapuk A.
 Chaivisuthangkura P.
 Svasti J.
 Kumar C.V.

Abstract

Photocleavage of -lysozyme and bovine serum albumin (BSA) by L-phenylalanine-1(1-pyrene) methylamide (PMA-L-Phe) is reported here. The chiral probe, PMA-L-Phe, has a positively charged side chain, while the previous probes carried a free carboxyl group. The yield of lysozyme cleavage by PMA-L-Phe is increased to 57% when compared to the previous probes, while the yield of BSA cleavage is reduced to <5%. Sequencing studies indicated that PMA-L-Phe cleaves lysozyme at a single site, between residues Trp108-Va1109. Absorption and fluorescence spectral data indicate that PMA-L-Phe binds to lysozyme and BSA with affinity constants (Kb) of 3.3×105 M-1 and 3.8×105 M-1, respectively. © 2005 Bentham Science Publishers Ltd.

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https://hdl.handle.net/20.500.14740/6080

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Scopus: Year 1983-2021

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