Cross‐Reactivity of Polyclonal Antibodies against <i>Canavalia ensiformis</i> (Jack Bean) Urease and <i>Helicobacter pylori</i> Urease Subunit A Fragments

Kamiński, Zbigniew J.; Relich, Inga; Konieczna, Iwona; Kaca, Wiesław; Kolesińska, Beata

doi:10.1002/cbdv.201700444

Cited by 6 publications

(19 citation statements)

References 44 publications

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“…The automatic SPOT method with the use of cellulose modified with 1,3,5-triazine derivative [12] was used to synthesize the library of collagen II fragments immobilized on cellulose. The 1,3,5-triazine derivative acts as a linker separating the peptide from the cellulose matrix and ensuring its appropriate exposure to interaction with antibodies [13].…”

Section: Resultsmentioning

confidence: 99%

Selection of Fragments of Collagen II Useful in Regenerative Medicine

Rosiak¹,

Becht²,

Czerchawy³

et al. 2022

Proceedings of the 36th European and the 12th International Peptide Symposium

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Section: Resultsmentioning

confidence: 99%

Selection of Fragments of Collagen II Useful in Regenerative Medicine

Rosiak¹,

Becht²,

Czerchawy³

et al. 2022

Proceedings of the 36th European and the 12th International Peptide Symposium

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“…The libraries of fragments of TGF-α, EGF, and VEGF A were obtained. The first stage of the synthetic work involved the incorporation of the isocyanurate derivative on the surface of the cellulose matrix [30,31] (Figure 1). As our research has shown, the isocyanurate derivatives can be used in the SPOT peptide synthesis (modified cellulose as a solid phase) according to the Fmoc/tBu strategy.…”

Section: Resultsmentioning

confidence: 99%

“…The epitope mapping of cTnI in combination with previous studies, conducted in our lab, resulted in the selection of four peptide sequences which are cTnI [19][20][21][22][23][24][25][26][27][28][29][30][31] , cTnI 66-77 , cTnI 110-122 , cTnI [118][119][120][121][122][123][124][125][126][127][128][129][130][131] . The synthesized conjugates are listed in Table 1.…”

Section: Resultsmentioning

confidence: 99%

Proceedings of the 36th European and the 12th International Peptide Symposium

2022

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On behalf of the organizing committee, we welcomed you to the 36th European and 12th International Peptide Symposium in Sitges (Barcelona), Spain, from August 28 to September 2, 2022. This was a great occasion to rejoin the international peptide family again after these uncertain times.The meeting. themed "From Peptides to the World", was an ideal occasion for academia and industry scientists from all over the world. It provided an opportunity to learn and discuss about the thriving field of peptide science, exchange ideas, create new alliances as well as to meet old friendsand make new friends.The 36 th EPS scientific committee had set out to assemble an exciting program with a broad range of topics covering, among others, advances in peptide chemistry and structure, bioactive peptides and their therapeutic applications, peptide biomaterials, and nanotechnology and delivery. In addition. more than 475 posters was the perfect environment to move peptide science ahead.The conference venue (Melia Sitges) was a pleasant setting for commercial exhibition, poster sessions and coffee breaks surrounded by outdoor pool gardens and terraces overlooking the Mediterranean Sea. Sitges, 40 km south of Barcelona, is a trendy resort with a privileged location and mild Mediterranean climate. Four kilometers of beach, fringed by a sea-front promenade dotted with artful colonial mansions facing the sea, provided a perfect excuse for strolling in this convivial town well-known for its open, inclusive, relaxed atmosphere.The scientific and local organizing committees, supported by the E P S executive committee, were keen to make the 36EPS/12IPS a memorable and successful scientific event. Convinced that your presence contributed to that we like to take the opportunity to thank you for your presence, continuing support and understanding during these difficult times.

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“…The plate was then washed with THF (3 × 10 mL), treated with a solution of Fmoc-Ala-OH (1.556 g, 5 mM) and NMM (0.55 mL, 5 mM) in dichloromethane (DCM, 20 mL) for 4 h, washed with DCM (5 × 10 mL), and then the excess solvent was removed. The plate was immersed in dry boiling toluene for 6 h and then dried thoroughly in a vacuum desiccator (Kaminski et al 2018). The Fmoc group was removed by treatment with a 25% solution of piperidine in dimethyl formamide (DMF, 20 mL) for 15 min followed by washing with DMF (2 × 10 mL) and DCM (2 × 10 mL).…”

Section: Immobilization Of Alanine On the Cellulose Platementioning

confidence: 99%

“…In earlier studies we revealed that Helicobacter pylori Ure A fragments 11-24, 21-33, and 31-42 were able to interact with Jack bean urease antibodies (Kaminski et al 2018).…”

Section: Introductionmentioning

confidence: 96%

Synthesis of Bacterial Urease Flap Region Peptide Equivalents and Detection of Rheumatoid Arthritis Antibodies Using Two Methods

Konieczna

Kolesińska

Gleńska-Olender

et al. 2019

Int J Pept Res Ther

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Rheumatoid arthritis (RA) is an autoimmune inflammatory disease that leads to cartilage damage, joint destruction and bone erosions. Serological analysis is one of the most important tools for diagnosis of RA. The aims of studies were the synthesis of an amino-acid library of epitope CHHLDKSIKEDVQFADSRI corresponding to the flap region of H. pylori urease and investigation recognition by serum antibodies from one rheumatoid arthritis patient (RAP) and one volunteer blood donor (VBD) tested by two semi-quantitative methods. In this study we compared two immunoblot variants for estimation of antibodies recognizing five synthetic peptides corresponding to the urease flap region sequence from different organisms. One immunoblot variant was a classic dot-blot using HRP-conjugated anti-human antibodies, where the level of bound immunoglobulins was estimated by digitization of color formed by reaction with secondary antibody. The second immunoblot variant was based on fluorescein-conjugated anti human antibodies. Both semi-quantitative methods were effective for evaluation of antibodies, and their advantages and disadvantages are discussed. To identify the amino-acid residues critical for reaction with antibodies, an amino-acid scan of the complete sequence of the flap region from Helicobacter pylori urease (epitope BK-61B) was conducted. Each sub-library (1-19) contained 19 peptides, each with different amino acids (a-w) at defined positions. All components of the library were synthesized using a divergent strategy. Patterns of serological reaction with the peptide library were unique for each serum sample from an RA patient or control blood donor. The amino-acid residues in epitope BK-61B necessary for strong reaction with antibodies and preventing reaction with antibodies were identified. Keywords Urease flap region peptides · Rheumatoid arthritis antibody detection Abbreviations RARheumatoid arthritis DCMT 2,4-Dichloro-6-methoxy-1,3,5-triazine RAP Rheumatoid arthritis serum VBD Volunteer blood donors serum

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Cross‐Reactivity of Polyclonal Antibodies against Canavalia ensiformis (Jack Bean) Urease and Helicobacter pylori Urease Subunit A Fragments

Cited by 6 publications

References 44 publications

Selection of Fragments of Collagen II Useful in Regenerative Medicine

Selection of Fragments of Collagen II Useful in Regenerative Medicine

Proceedings of the 36th European and the 12th International Peptide Symposium

Synthesis of Bacterial Urease Flap Region Peptide Equivalents and Detection of Rheumatoid Arthritis Antibodies Using Two Methods

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