Designed Nanocage Displaying Ligand-Specific Peptide Bunches for High Affinity and Biological Activity

ACS Nano ◽  
2013 ◽  
Vol 7 (9) ◽  
pp. 7462-7471 ◽  
Author(s):  
Jae Og Jeon ◽  
Soyoun Kim ◽  
Eunsu Choi ◽  
Kihyuk Shin ◽  
Kiweon Cha ◽  
...  
Keyword(s):  
Biological Activity ◽  
High Affinity ◽  
Specific Peptide

Synthesis and biological activity of high-affinity retinoic acid receptor antagonists

1999 ◽  
Vol 7 (7) ◽  
pp. 1321-1338 ◽  
Author(s):  
Alan T. Johnson ◽  
Liming Wang ◽  
Andrew M. Standeven ◽  
Maria Escobar ◽  
Roshantha A.S. Chandraratna
Keyword(s):  
Biological Activity ◽  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
Receptor Antagonists ◽  
Acid Receptor ◽  
High Affinity

Phage Display as A Bio-Technique for Cancer Immunotherapy

2020 ◽  
Vol 17 (4) ◽  
pp. 379-387
Author(s):  
Shirin Mahmoodi ◽  
Navid Nezafat ◽  
Younes Ghasemi
Keyword(s):  
Phage Display ◽  
Cancer Immunotherapy ◽  
Tumor Antigens ◽  
High Affinity ◽  
Phage Antibodies ◽  
Phage Display Libraries ◽  
Antigen Presenting ◽  
Immunogenic Properties ◽  
Specific Peptide ◽  
Selection Of

Background: Phage display is a biotechnological technique that presents peptides with coated proteins on the surface of phage. In the last two decades, growing applications of phage display in various fields of biotechnology have been investigated. Phage display libraries allow to present billions of peptides on phage surface for selection of a specific peptide with the desired affinity. Objective: In this regard, high-affinity phage antibodies against tumor antigens are produced and applied for diagnosis and treatment of cancer. Method: Moreover, phage display libraries are employed to select the high affinity T Cell Receptors (TCRs) for the peptide-MHC complex which is an attractive approach in cancer immunotherapy. Due to immunogenic properties of phage particles, phage-based vaccines do not require adjuvant, in addition the phage particles can effectively take up by Antigen Presenting Cells (APCs). Results: Taken together, phage-based cancer vaccines are ideal candidates that provide a key for eradication of tumor cells. Conclusion: In this review, we focus on various applications of a phage display platform in different types of cancer immunotherapy approaches.

scholarly journals The Specificity of Peptides Bound to Human Histocompatibility Leukocyte Antigen (HLA)-B27 Influences the Prevalence of Arthritis in HLA-B27 Transgenic Rats

1998 ◽  
Vol 188 (5) ◽  
pp. 877-886 ◽  
Author(s):  
Ming Zhou ◽  
Alain Sayad ◽  
William A. Simmons ◽  
Richard C. Jones ◽  
Shanna D. Maika ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Rheumatic Diseases ◽  
Hla B27 ◽  
Spleen Cells ◽  
Transgenic Rats ◽  
Leukocyte Antigen ◽  
High Affinity ◽  
Peptide Fraction ◽  
Specific Peptide ◽  
Control Construct

Human histocompatibility leukocyte antigen B27 is highly associated with the rheumatic diseases termed spondyloarthropathies, but the mechanism is not known. B27 transgenic rats develop a spontaneous disease resembling the human spondyloarthropathies that includes arthritis and colitis. To investigate whether this disease requires the binding of specific peptides to B27, we made a minigene construct in which a peptide from influenza nucleoprotein, NP383-391 (SRYWAIRTR), which binds B27 with high affinity, is targeted directly to the ER by the signal peptide of the adenovirus E3/gp19 protein. Rats transgenic for this minigene, NP1, were made and bred with B27 rats. The production of the NP383-391 peptide in B27+NP1+ rats was confirmed immunologically and by mass spectrometry. The NP1 product displaced ∼90% of the 3H-Arg-labeled endogenous peptide fraction in B27+NP1+ spleen cells. Male B27+NP1+ rats had a significantly reduced prevalence of arthritis, compared with B27+NP− males or B27+ males with a control construct, NP2, whereas colitis was not significantly affected by the NP1 transgene. These findings support the hypothesis that B27-related arthritis requires binding of a specific peptide or set of peptides to B27, and they demonstrate a method for efficient transgenic targeting of peptides to the ER.

Synthesis, biological activity and molecular modelling of new trisubstituted 8-azaadenines with high affinity for A1 adenosine receptors

2007 ◽  
Vol 42 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Irene Giorgi ◽  
Anna Maria Bianucci ◽  
Giuliana Biagi ◽  
Oreste Livi ◽  
Valerio Scartoni ◽  
...  
Keyword(s):  
Biological Activity ◽  
Molecular Modelling ◽  
Adenosine Receptors ◽  
High Affinity ◽  
A1 Adenosine Receptors

scholarly journals Studies on the Interactions of 3,11-Difluoro-6,8,13-trimethyl-8H-quino[4,3,2-kl]acridinium and Insulin with the Quadruplex-Forming Oligonucleotide Sequence a2 from the Insulin-Linked Polymorphic Region

Molecules ◽  
2021 ◽  
Vol 26 (21) ◽  
pp. 6595
Author(s):  
Peter Jonas Wickhorst ◽  
Heiko Ihmels ◽  
Thomas Paululat
Keyword(s):  
Biological Activity ◽  
Promoter Region ◽  
Spectroscopic Studies ◽  
Polymorphic Region ◽  
Quadruplex Dna ◽  
Preferential Formation ◽  
High Affinity ◽  
Quadruplex Structure ◽  
G4 Dna ◽  
Oligonucleotide Sequence

Recently, several quadruplex-DNA-forming sequences have been identified in the insulin-linked polymorphic region (ILPR), which is a guanine-rich oligonucleotide sequence in the promoter region of insulin. The formation of this non-canonical quadruplex DNA (G4-DNA) has been shown to be involved in the biological activity of the ILPR, specifically with regard to its interplay with insulin. In this context, this contribution reports on the investigation of the association of the quadruplex-forming ILPR sequence a2 with insulin as well as with the well-known G4-DNA ligand 3,11-difluoro-6,8,13-trimethyl-8H-quino[4,3,2-kl]acridinium (1), also named RHPS4, by optical and NMR spectroscopy. CD- and NMR-spectroscopic measurements confirmed the preferential formation of an antiparallel quadruplex structure of a2 with four stacked guanine quartets. Furthermore, ligand 1 has high affinity toward a2 and binds by terminal π stacking to the G1–G11–G15–G25 quartet. In addition, the spectroscopic studies pointed to an association of insulin to the deoxyribose backbone of the loops of a2.

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