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Main Title: Photochemical formation of quinone methides from peptides containing modified tyrosine
Author(s): Husak, Antonija
Noichl, Benjamin P.
Ramljak, Tatjana Šumanovac
Sohora, Margareta
Škalamera, Đani
Budiša, Nediljko
Basarić, Nikola
Type: Article
Language Code: en
Abstract: We have demonstrated that quinone methide (QM) precursors can be introduced in the peptide structure and used as photoswitchable units for peptide modifications. QM precursor 1 was prepared from protected tyrosine in the Mannich reaction, and further used as a building block in peptide synthesis. Moreover, peptides containing tyrosine can be transformed into a photoactivable QM precursor by the Mannich reaction which can afford monosubstituted derivatives 2 or bis-substituted derivatives 3. Photochemical reactivity of modified tyrosine 1 and dipeptides 2 and 3 was studied by preparative irradiation in CH3OH where photodeamination and photomethanolysis occur. QM precursors incorporated in peptides undergo photomethanolysis with quantum efficiency phi(R) = 0.1-0.2, wherein the peptide backbone does not affect their photochemical reactivity. QMs formed from dipeptides were detected by laser flash photolysis (lambda(max) approximate to 400 nm, iota = 100 mu s- 20 ms) and their reactivity with nucleophiles was studied. Consequently, QM precursors derived from tyrosine can be a part of the peptide backbone which can be transformed into QMs upon electronic excitation, leading to the reactions of peptides with different reagents. This proof of principle showing the ability to photochemically trigger peptide modifications and interactions with other molecules can have numerous applications in organic synthesis, materials science, biology and medicine.
Issue Date: 2016
Date Available: 24-Oct-2017
DDC Class: 540 Chemie und zugeordnete Wissenschaften
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Journal Title: Organic & biomolecular chemistry : OBC
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 14
Issue: 46
Publisher DOI: 10.1039/c6ob02191c
Page Start: 10894
Page End: 10905
EISSN: 1477-0539
ISSN: 1477-0520
Appears in Collections:Fachgebiet Biokatalyse » Publications

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