Sinéad M. Ryan

Dr. Sinéad M. Ryan

orcid

Research Focus & Metrics

Academic Career Length

19Years (2008-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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21 April 2008 in Expert Opinion on Drug Delivery
Verified
Journal Article
Closed access
SRSinéad M. Ryan
Sinéad M. Ryan
Giuseppe MantovaniGiuseppe Mantovani
Giuseppe Mantovani
XWXuexuan Wang
Xuexuan Wang
DHDavid M Haddleton
David M Haddleton
David BraydenDavid Brayden
David Brayden
Background: Although various injected peptide and protein therapeutics have been developed successfully over the past 25 years, several pharmacokinetic and immunological challenges are still encountered that can limit the efficacy of both novel and established biotech molecules. Objective and method: PEGylation is a popular technique to address such properties. PEGylated drugs exhibit prolonged half-life, higher stability, water solubility, lower immunogenicity and antigenicity, as well as potential for specific cell targeting. Although PEGylated drug conjugates have been on the market for many years, the technology has steadily developed in respect of site-specific chemistry, chain length, molecular weights and purity of conjugate. These developments have occurred in parallel to improvements in physicochemical methods of characterization. Conclusion: This review will discuss recent achievements in PEGylation processes with an emphasis on novel PEG-drugs constructs, the unrealized potential of PEGylation ...

21 December 2009 in Biomacromolecules
Verified
Journal Article
Closed access
LRLee-Anne B. Rawlinson
Lee-Anne B. Rawlinson
SRSinéad M. Ryan
Sinéad M. Ryan
Giuseppe MantovaniGiuseppe Mantovani
Giuseppe Mantovani
JSJay A. Syrett
Jay A. Syrett
DHDavid M. Haddleton
David M. Haddleton
David BraydenDavid Brayden
David Brayden

12 April 2012 in Journal of the American Chemical Society
Verified
Journal Article
Closed access
MJMathew W. Jones
Mathew W. Jones
Giuseppe MantovaniGiuseppe Mantovani
Giuseppe Mantovani
CBClaudia A. Blindauer
Claudia A. Blindauer
SRSinéad M. Ryan
Sinéad M. Ryan
XWXuexuan Wang
Xuexuan Wang
DHDavid M. Haddleton
David M. Haddleton

1 July 2016 in Trends in Food Science & Technology
Verified
Journal Article
Closed access
JGJohn Gleeson
John Gleeson
SRSinéad M. Ryan
Sinéad M. Ryan
David BraydenDavid Brayden
David Brayden

1 January 2009 in Chemical Communications
Verified
Journal Article
Closed access
PDF file
MJMathew W. Jones
Mathew W. Jones
Giuseppe MantovaniGiuseppe Mantovani
Giuseppe Mantovani
SRSinéad M. Ryan
Sinéad M. Ryan
XWXuexuan Wang
Xuexuan Wang
David BraydenDavid Brayden
David Brayden
DHDavid M. Haddleton
David M. Haddleton
We employ water-soluble organic phosphines as key reagents in a one-pot synthetic protocol where a (poly)peptide disulfide bridge is first reduced followed by subsequent reaction of the two thiols in situ with poly(monomethoxy ethylene glycol)(meth)acrylates (p(mPEG)(M)A); we use salmon calcitonin (sCT) as a disulfide bridge-containing peptide, which contains a disulfide bridge—Cys1–Cys7—that can be reduced to give two sulfhydryl units available for thiol functionalisation; bioactivity is retained.

15 October 2008 in Applied and Environmental Microbiology
Verified
Journal Article
Open access
PDF file
MMMary O’connell O’Connell Motherway
Mary O’connell O’Connell Motherway
GFGerald F. Fitzgerald
Gerald F. Fitzgerald
SNSabine Neirynck
Sabine Neirynck
SRSinéad M. Ryan
Sinéad M. Ryan
LSLothar Steidler
Lothar Steidler
DSDouwe Sinderen
Douwe Sinderen
The apuB gene of Bifidobacterium breve UCC2003 was shown to encode an extracellular amylopullulanase. ApuB is composed of a distinct N-terminally located α-amylase-containing domain which hydrolyzes α-1,4-glucosidic linkages in starch and related polysaccharides and a C-terminally located pullulanase-containing domain which hydrolyzes α-1,6 linkages in pullulan, allowing the classification of this enzyme as a bifunctional class II pullulanase. A knockout mutation of the apuB gene in B. breve UCC2003 rendered the resulting mutant incapable of growth in medium containing starch, amylopectin, glycogen, or pullulan as the sole carbon and energy source, confirming the crucial physiological role of this gene in starch metabolism.