The way in which professor Michael Przybylski has combined the spirit of research with entrepreneurship has set an example for any and all scientists. He has made significant achievements in the fields of mass spectrometry, biochemistry and medicine, and has initiated important technological developments in the area of protein analysis. Between 2016 and 2023 professor Przybylski's scientific focus shifted on protein interactions with emphasis on aptamer-protein and antibody-protein analysis. This review focuses on professor Przybylski's achievements in the last few years highlighting his impact on the scientific community, on his students and colleagues.
GlockerMOLupuLMPetreBA. Michael Przybylski (1948–2023) devoted half a century to mass spectrometry. J Am Soc Mass Spectrom2023; 34: 1957–1961.
2.
RosenFSSteinerLAUnanueER. Macmillan dictionary of immunology. New York, NY: Macmillan, 1989, p. 223.
3.
RasmussenIBLundeEMichaelsenTE, et al.The principle of delivery of T cell epitopes to antigen-presenting cells applied to peptides from influenza virus, ovalbumin, and hen egg lysozyme: implications for peptide vaccination. Proc Natl Acad Sci U S A2001; 98: 10296–10301.
4.
BrineyBInderbitzinAJoyceC,et al.Commonality despite exceptional diversity in the baseline human antibody repertoire. Nature2019; 566: 393–397.
5.
Van OssCJ. Hydrophobic, hydrophilic and other interactions in epitope-paratope binding. Mol Immunol1995; 32: 199–211.
6.
BílkováZStefanescuRCecalR, et al.Epitope extraction technique using a proteolytic magnetic reactor combined with Fourier-transform ion cyclotron resonance mass spectrometry as a tool for the screening of potential vaccine lead peptides. Eur J Mass Spectrom (Chichester)2005; 11: 489–495.
7.
JuszczykPParaschivGSzymanskaA, et al.Binding epitopes and interaction structure of the neuroprotective protease inhibitor cystatin C with beta-amyloid revealed by proteolytic excision mass spectrometry and molecular docking simulation. J Med Chem2009; 52: 2420–2428.
8.
MafteiMTianXManeaM, et al.Interaction structure of the complex between neuroprotective factor humanin and Alzheimer's β-amyloid peptide revealed by affinity mass spectrometry and molecular modeling. J Pept Sci2012; 18: 373–382.
9.
SaulFAPoljakRJ. Structural patterns at residue positions 9, 18, 67 and 82 in the VH framework regions of human and murine immunoglobulins. J Mol Biol1993; 230: 15–20.
10.
TuTDrăguşanuMPetreBA, et al.Protein-peptide affinity determination using an h/d exchange dilution strategy: application to antigen-antibody interactions. J Am Soc Mass Spectrom2010; 21: 1660–1667.
11.
O'LearyTRBalasubramaniamDHughesK, et al.Hydrogen-deuterium exchange epitope mapping of glycosylated epitopes enabled by online immobilized glycosidase. Anal Chem2023; 95: 10204–10210.
12.
YefremovaYOpuniKFMDanquahBD, et al.Intact transition epitope mapping (ITEM). J Am Soc Mass Spectrom2017; 28: 1612–1622.
13.
OpuniKFMAl-MajdoubMYefremovaY, et al.Mass spectrometric epitope mapping. Mass Spectrom Rev2018; 37: 229–241.
14.
MorgnerNBarthHDBrutschyB, et al.Binding sites of the viral RNA element TAR and of TAR mutants for various peptide ligands, probed with LILBID: a new laser mass spectrometry. J Am Soc Mass Spectrom2008; 19: 1600–1611.
15.
BrandstätterLSokolovaLEicherT, et al.Analysis of AcrB and AcrB/DARPin ligand complexes by LILBID MS. Biochim Biophys Acta2011; 1808: 2189–2196.
16.
LiGSuzukiHTanakaT, et al.Epitope mapping of an Anti-EpCAM monoclonal antibody (EpMab-37) using the alanine scanning method. Monoclon Antib Immunodiagn Immunother2023; 42: 41–47.
17.
MachtMFiedlerWKürzingerK,et al.Mass spectrometric mapping of protein epitope structures of myocardial infarct markers myoglobin and troponin T. Biochemistry1996; 35: 15633–9.
18.
MihocDLupuLMWiegandP, et al.Antibody epitope and affinity determination of the myocardial infarction marker myoglobin by SPR-biosensor mass spectrometry. J Am Soc Mass Spectrom2021; 32: 106–113.
19.
PeetzOHellwigNHenrichE, et al.LILBID And nESI: different native mass spectrometry techniques as tools in structural biology. J Am Soc Mass Spectrom2019; 30: 181–191.
20.
DouganDAMalbyRLGruenLC, et al.Effects of substitutions in the binding surface of an antibody on antigen affinity. Protein Eng1998; 11: 65–74.
21.
NahsholOBronnerVNotcovichA, et al.Parallel kinetic analysis and affinity determination of hundreds of monoclonal antibodies using the ProteOn XPR36. Anal Biochem2008; 383: 52–60.
22.
PolEKarlssonRRoosH, et al.Biosensor-based characterization of serum antibodies during development of an anti-IgE immunotherapeutic against allergy and asthma. J Mol Recognit2007; 20: 22–31.
SlamnoiuSVladCStumbaumM, et al.Identification and affinity-quantification of ß-amyloid and α-synuclein polypeptides using on-line SAW-biosensor-mass spectrometry. Am Soc Mass Spectrom2014; 25: 1472–1481.
PetreBA, et al.When is mass spectrometry combined with affinity approaches essential? A case study of tyrosine nitration in proteins. J Am Soc Mass Spectrom2012; 23: 1831–1840.
27.
Epitop- und Affinitätsbestimmung von Protein-Antikörper-Wechselwirkungen mittels Affinitäts-Massenspektrometrie, Spectroscopy, 2023.
28.
van DyckCH. Anti-amyloid-β monoclonal antibodies for Alzheimer's disease: pitfalls and promise. Biol Psychiatry2018; 83: 311–319.
29.
ParaschivGVinckeCCzaplewskacP, et al.Epitope structure and binding affinity of single chain llama anti-ß-amyloid antibodies revealed by proteolytic excision affinity-mass spectrometry. Mol Recognition2013; 26: 1–9.
30.
LiebleinTZanglRMartinJ, et al.Structural rearrangement of amyloid-β upon inhibitor binding suppresses formation of Alzheimer’s disease related oligomers. eLife2020; 9: e59306.
31.
ZanglRMorgnerN. Wie kleine amyloid-β-peptide zum großen problem im Gehirn werden können. Biospektrum2021; 27: 705–708.
32.
Soria LopezJAGonzálezHMLégerGC. Alzheimer's disease. Handb Clin Neurol2019; 167: 231–255.
33.
ȘtefănescuRLupuLManeaM, et al.Molecular characterization of the β-amyloid (4–10) epitope of plaque specific Aβ antibodies by affinity-mass spectrometry using alanine site mutation. J Pept Sci2018; 24.
34.
OhashiTIizukaSIdaH,et al.Reduced alpha-Gal A enzyme activity in Fabry fibroblast cells and fabry mice tissues induced by serum from antibody positive patients with Fabry disease. Mol Genet Metab2008; 94: 313–318.
35.
GermainDPElliottPMFalissardB, et al.The effect of enzyme replacement therapy on clinical outcomes in male patients with Fabry disease: a systematic literature review by a European panel of experts. Mol Genet Metab Rep2019; 19: 100454.
36.
KukackaZIurascuMLupuL, et al.Antibody pitope of human α-galactosidase A eevealed by affinity mass spectrometry: a basis for reversing immunoreactivity in enzyme replacement therapy of Fabry disease. ChemMedChem2018; 13: 909–915.
37.
LupuLMWiegandPHoldschickD, et al.Identification and affinity determination of protein-antibody and protein-aptamer epitopes by biosensor-mass spectrometry combination. Int J Mol Sci2021; 22: 12832.
38.
WiegandP, et al.Epitope identification and affinity determination of an inhibiting human antibody to interleukin IL8 (CXCL8) by SPR- biosensor−mass spectrometry combination. J Am Soc Mass Spectrom2020; 31: 109.
39.
TianXCecalRAmstaldenER, et al.Synthesis, structural characterisation and epitope elucidation of the cytoplasmic domain of Alzheimer's amyloid precursor protein by FTICR mass spectrometry. J Peptide Sci2002; 8: 182.
40.
MihocD, et al.Antibody epitope and affinity determination of the myocardial infarction marker myoglobin by SPR-biosensor mass spectrometry. J Am Soc Mass Spectrom2021; 32: 106–113.
41.
MachtMFiedlerWKürzingerK,et al.Mass spectrometric mapping of protein epitope structures of myocardial infarct markers myoglobin and troponin T. Biochemistry1996; 35: 15633–9.
42.
TramarinANaldiMDeganiG, et al.Unveiling the molecular mechanisms underpinning biorecognition of early-glycated human serum albumin and receptor for advanced glycation end products. Anal Bioanal Chem2020; 412: 4245–4259.
43.
RinaldiFLupuLRuscheH, et al.Epitope and affinity determination of recombinant mycobacterium tuberculosis Ag85B antigen towards anti-Ag85 antibodies using proteolytic affinity-mass spectrometry and biosensor analysis. Anal Bioanal Chem2019; 411: 439–448.
44.
BaschungYLupuLMoiseA, et al.Epitope ligand binding sites of blood group oligosaccharides in lectins revealed by pressure-assisted proteolytic excision affinity mass spectrometry. J Am Soc Mass Spectrom2018; 29: 1881–1891.
45.
ZhaoNPeiSNParekhP, et al.Blocking interaction of viral gp120 and CD4-expressing T cells by single-stranded DNA aptamers. Int J Biochem Cell Biol2014; 51: 10–18.
46.
KohlbergerMGadermaierG. SELEX: critical factors and optimization strategies for successful aptamer selection. Biotechnol Appl Biochem2022; 69: 1771–1792.
47.
MengWChenT. Association between the HGF/c-MET signaling pathway and tumorigenesis, progression and prognosis of hepatocellular carcinoma (review). Oncol Rep2021; 46: 191.
48.
UekiRSandoS. A DNA aptamer to c-Met inhibits cancer cell migration. Chem Commun (Camb)2014; 50: 13131–4.
49.
LupuL, et al.Molecular epitope determination of aptamer complexes of the multidomain protein C-met by proteolytic affinity-mass spectrometry. ChemMedChem2020; 15: 363–369.
50.
DanquahBDYefremovaYOpuniKFM, et al.Intact transition epitope mapping–thermodynamic weak-force order (ITEM–TWO). J Proteomics2020; 212: 103572.
51.
DanquahBDRöwerCOpuniKM, et al.Intact transition epitope mapping–targeted high-energy rupture of extracted epitopes (ITEM-THREE). Mol Cell Proteomics2019; 18: 1543–1555.
52.
ZammataroAKoyCRußM, et al.Intact transition epitope mapping-serological inspection by epitope EXtraction (ITEM-SIX). Molecules2023; 28: 3092.
53.
MorgnerNKleinschrothTBarthHD, et al.A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J Am Soc Mass Spectrom2007; 18: 1429–1438.
54.
YoungPHenseGImmerC, et al.LILBID laser dissociation curves: a mass spectrometry-based method for the quantitative assessment of dsDNA binding affinities. Sci Rep2020; 10: 20398.
55.
HenrichEPeetzOHeinC, et al.Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biology. Elife2017; 6: e20954.
