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EP38461
Poster Title: Studying human haptoglobin hemoglobin structure and interactions using H/D exchange and timsTOF Pro.
Submitted on 09 Mar 2022
Author(s): Pavla Vankova 1 , Petr Man 1 , Petr Pompach 1 , Stuart Pengelley 2 , Gary Kruppa 3 , Daniel Kavan 1 , Petr Novak 1
Affiliations: 1 Laboratory of Structural Biology and Cell Signaling ( aka Peterslab ), Institute of Microbiology of the Czech Acad Sci , Prague, CZ 2 Bruker Daltonik GmbH, Bremen, Germany 3 Bruker s.r.o ., Brno, CZ
Poster Views: 99
Submitted on 09 Mar 2022
Author(s): Pavla Vankova 1 , Petr Man 1 , Petr Pompach 1 , Stuart Pengelley 2 , Gary Kruppa 3 , Daniel Kavan 1 , Petr Novak 1
Affiliations: 1 Laboratory of Structural Biology and Cell Signaling ( aka Peterslab ), Institute of Microbiology of the Czech Acad Sci , Prague, CZ 2 Bruker Daltonik GmbH, Bremen, Germany 3 Bruker s.r.o ., Brno, CZ
Poster Views: 99
Abstract: HDX-MS workflow was successfully adopted to timsTOF Pro with PASEF and provides very significant improvement in terms of identified peptides = higher resolution in HDX-MS
So far, Hp 1-1 and Hp 2-2 were compared in their binding to hemoglobin and showed different extent of protection on the Hp Hb interaction interface hich aligns well with their know different affinities.
While desialylation of the N-glycans had no or very small effect on the structure/interaction, complete removal of the glycan likely alters the Hp-Hb contact and Hp structure This fits to a recent independent study published in PNAS last year doi 10 1073 /pnas 2002483117 Further investigation is now being carried out.
Interaction of Hp-Hb in the whole serum was partially optimized. Now sera phenotyping is carried out to select samples matching the individual forms And will be subjected to the HDX workflow done with individual proteins.
All results will be then integrated with the data from other structural MS techniques being gather by the members of peterslab.Summary: HDX-MS workflow was successfully adopted to timsTOF Pro with PASEF and provides very significant improvement in terms of identified peptides = higher resolution in HDX-MSReferences: Lab Members
Pavla Vaňková
Petr Pompach
Daniel Kavan
Dmitry Loginov
Zdenek Kukacka
Josef Chmelik
Petr Novák
Collaborators from Bruker
Stuart Pengelley
Gary Kruppa
So far, Hp 1-1 and Hp 2-2 were compared in their binding to hemoglobin and showed different extent of protection on the Hp Hb interaction interface hich aligns well with their know different affinities.
While desialylation of the N-glycans had no or very small effect on the structure/interaction, complete removal of the glycan likely alters the Hp-Hb contact and Hp structure This fits to a recent independent study published in PNAS last year doi 10 1073 /pnas 2002483117 Further investigation is now being carried out.
Interaction of Hp-Hb in the whole serum was partially optimized. Now sera phenotyping is carried out to select samples matching the individual forms And will be subjected to the HDX workflow done with individual proteins.
All results will be then integrated with the data from other structural MS techniques being gather by the members of peterslab.Summary: HDX-MS workflow was successfully adopted to timsTOF Pro with PASEF and provides very significant improvement in terms of identified peptides = higher resolution in HDX-MSReferences: Lab Members
Pavla Vaňková
Petr Pompach
Daniel Kavan
Dmitry Loginov
Zdenek Kukacka
Josef Chmelik
Petr Novák
Collaborators from Bruker
Stuart Pengelley
Gary Kruppa
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