Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification

Nicola McMillan; Jesus M. De La Fuente; Alexis D.C. Parenty; Nikolaj Gadegaard; Andrew R. Pitt; Katrina Thomson; Cameron MacKenzie; Sharon M. Kelly; Leroy Cronin

doi:10.1039/b702575k

Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification

Nicola McMillan
, Jesus M. De La Fuente
, Alexis D.C. Parenty
, Nikolaj Gadegaard
, Andrew R. Pitt
, Katrina Thomson
, Cameron MacKenzie
, Sharon M. Kelly
, Leroy Cronin^*

^*Corresponding author for this work

Analytical, Measurements and Physical Chemistry

University of Glasgow
Universidad de Zaragoza

Research output: Contribution to journal › Article › peer-review

Abstract

N-Heterocyclic cations are incorporated into proteins using 5-(2-bromoethyl)phenanthridinium bromide, which selectively reacts with either cysteine or lysine residues, resulting in ethylphenanthridinium (Phen) or highly stable cyclised dihydro-imidazo-phenanthridinium (DIP) adducts respectively; these modifications have been found to manipulate the observed structure of lysozyme and bovine serum albumin by AFM.

Original language	English
Pages (from-to)	2581-2583
Number of pages	3
Journal	Chemical Communications
Volume	2007
Issue number	25
DOIs	https://doi.org/10.1039/b702575k
Publication status	Published - 29 May 2007

Access to Document

10.1039/b702575k

Cite this

@article{4407fc9b9f384d2593fd905fd976730b,

title = "Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification",

abstract = "N-Heterocyclic cations are incorporated into proteins using 5-(2-bromoethyl)phenanthridinium bromide, which selectively reacts with either cysteine or lysine residues, resulting in ethylphenanthridinium (Phen) or highly stable cyclised dihydro-imidazo-phenanthridinium (DIP) adducts respectively; these modifications have been found to manipulate the observed structure of lysozyme and bovine serum albumin by AFM.",

author = "Nicola McMillan and \{De La Fuente\}, \{Jesus M.\} and Parenty, \{Alexis D.C.\} and Nikolaj Gadegaard and Pitt, \{Andrew R.\} and Katrina Thomson and Cameron MacKenzie and Kelly, \{Sharon M.\} and Leroy Cronin",

year = "2007",

month = may,

day = "29",

doi = "10.1039/b702575k",

language = "English",

volume = "2007",

pages = "2581--2583",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "25",

}

TY - JOUR

T1 - Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification

AU - McMillan, Nicola

AU - De La Fuente, Jesus M.

AU - Parenty, Alexis D.C.

AU - Gadegaard, Nikolaj

AU - Pitt, Andrew R.

AU - Thomson, Katrina

AU - MacKenzie, Cameron

AU - Kelly, Sharon M.

AU - Cronin, Leroy

PY - 2007/5/29

Y1 - 2007/5/29

N2 - N-Heterocyclic cations are incorporated into proteins using 5-(2-bromoethyl)phenanthridinium bromide, which selectively reacts with either cysteine or lysine residues, resulting in ethylphenanthridinium (Phen) or highly stable cyclised dihydro-imidazo-phenanthridinium (DIP) adducts respectively; these modifications have been found to manipulate the observed structure of lysozyme and bovine serum albumin by AFM.

AB - N-Heterocyclic cations are incorporated into proteins using 5-(2-bromoethyl)phenanthridinium bromide, which selectively reacts with either cysteine or lysine residues, resulting in ethylphenanthridinium (Phen) or highly stable cyclised dihydro-imidazo-phenanthridinium (DIP) adducts respectively; these modifications have been found to manipulate the observed structure of lysozyme and bovine serum albumin by AFM.

UR - https://www.scopus.com/pages/publications/34250734517

U2 - 10.1039/b702575k

DO - 10.1039/b702575k

M3 - Article

C2 - 17579744

AN - SCOPUS:34250734517

SN - 1359-7345

VL - 2007

SP - 2581

EP - 2583

JO - Chemical Communications

JF - Chemical Communications

IS - 25

ER -

Incorporation of N-heterocyclic cations into proteins with a highly directed chemical modification

Abstract

Access to Document

Other files and links

Fingerprint

Cite this