Sakonwan Kuhaudomlarp
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Explore the profile of Sakonwan Kuhaudomlarp including associated specialties, affiliations and a list of published articles.
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Citations
206
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Recent Articles
11.
Kuhaudomlarp S, Cerofolini L, Santarsia S, Gillon E, Fallarini S, Lombardi G, et al.
Chem Sci
. 2021 Jun;
11(47):12662-12670.
PMID: 34094460
Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen ....
12.
Kuhaudomlarp S, Siebs E, Shanina E, Topin J, Joachim I, Gomes P, et al.
Angew Chem Int Ed Engl
. 2020 Dec;
60(15):8104-8114.
PMID: 33314528
Because of the antimicrobial resistance crisis, lectins are considered novel drug targets. Pseudomonas aeruginosa utilizes LecA and LecB in the infection process. Inhibition of both lectins with carbohydrate-derived molecules can...
13.
Zahorska E, Kuhaudomlarp S, Minervini S, Yousaf S, Lepsik M, Kinsinger T, et al.
Chem Commun (Camb)
. 2020 Jul;
56(62):8822-8825.
PMID: 32628229
Chronic infections with Pseudomonas aeruginosa are associated with the formation of bacterial biofilms. The tetrameric P. aeruginosa lectin LecA is a virulence factor and an anti-biofilm drug target. Increasing the...
14.
Kuhaudomlarp S, Gillon E, Varrot A, Imberty A
Methods Mol Biol
. 2020 Apr;
2132:257-266.
PMID: 32306333
LecA/PA-IL (Pfam PF07828) is a soluble galactose-binding lectin from bacterium Pseudomonas aeruginosa. The lectin is specific for α-galactose present on glycosphingolipids of the globoside family and has therefore been proposed...
15.
Singh R, Pergolizzi G, Nepogodiev S, de Andrade P, Kuhaudomlarp S, Field R
Chembiochem
. 2019 Oct;
21(7):1043-1049.
PMID: 31657512
The enzymatic synthesis of oligosaccharides depends on the availability of suitable enzymes, which remains a limitation. Without recourse to enzyme engineering or evolution approaches, herein we demonstrate the ability of...
16.
Lepsik M, Sommer R, Kuhaudomlarp S, Lelimousin M, Paci E, Varrot A, et al.
Eur J Med Chem
. 2019 May;
177:212-220.
PMID: 31146126
Pathogenic micro-organisms utilize protein receptors (lectins) in adhesion to host tissues, a process that in some cases relies on the interaction between lectins and human glycoconjugates. Oligosaccharide epitopes are recognized...
17.
Kuhaudomlarp S, Stevenson C, Lawson D, Field R
Proteins
. 2019 May;
87(10):885-892.
PMID: 31134667
Glycoside phosphorylases (GPs) with specificity for β-(1 → 3)-gluco-oligosaccharides are potential candidate biocatalysts for oligosaccharide synthesis. GPs with this linkage specificity are found in two families thus far-glycoside hydrolase family...
18.
Wagstaff B, Rejzek M, Kuhaudomlarp S, Hill L, Mascia I, Nepogodiev S, et al.
J Biol Chem
. 2019 Apr;
294(23):9172-9185.
PMID: 31010825
The 6-deoxy sugar l-rhamnose (l-Rha) is found widely in plant and microbial polysaccharides and natural products. The importance of this and related compounds in host-pathogen interactions often means that l-Rha...
19.
Kuhaudomlarp S, Pergolizzi G, Patron N, Henrissat B, Field R
J Biol Chem
. 2019 Mar;
294(16):6483-6493.
PMID: 30819804
Glycoside phosphorylases (GPs) catalyze the phosphorolysis of glycans into the corresponding sugar 1-phosphates and shortened glycan chains. Given the diversity of natural β-(1→3)-glucans and their wide range of biotechnological applications,...
20.
Kuhaudomlarp S, Walpole S, Stevenson C, Nepogodiev S, Lawson D, Angulo J, et al.
Chembiochem
. 2018 Jun;
20(2):181-192.
PMID: 29856496
Glycoside phosphorylases (GPs) carry out a reversible phosphorolysis of carbohydrates into oligosaccharide acceptors and the corresponding sugar 1-phosphates. The reversibility of the reaction enables the use of GPs as biocatalysts...