Self-Assembly of Bovine Ribonuclease A Triggered by Tyrosine Mediated Photo-Reduction of Disulfide Bonds

2016 ◽  
Vol 8 (6) ◽  
pp. 1314-1319
Author(s):  
Jinbing Xie ◽  
Zhonglin Wei ◽  
Xinfei Huang ◽  
Yi Cao ◽  
Meng Qin ◽  
...  
Keyword(s):  
Self Assembly ◽  
Disulfide Bonds ◽  
Ribonuclease A

Self-assembly of biomolecules at surfaces characterized by NEXAFS

2007 ◽  
Vol 85 (10) ◽  
pp. 793-800 ◽  
Author(s):  
Xiaosong Liu ◽  
Fan Zheng ◽  
A Jürgensen ◽  
V Perez-Dieste ◽  
D Y Petrovykh ◽  
...  
Keyword(s):  
Surface Science ◽  
Self Assembly ◽  
Ribonuclease A ◽  
Polarization Dependence ◽  
Biological Molecules ◽  
Self Assembled Monolayers ◽  
Peptide Bonds ◽  
Molecular Adsorbates ◽  
Dna Oligonucleotides ◽  
Assembled Monolayers

Surface science has made great strides towards tailoring surface properties via self-assembly of nanoscale molecular adsorbates. It is now possible to functionalize surfaces with complex biomolecules such as DNA and proteins. This brief overview shows how NEXAFS (near edge X-ray absorption fine structure spectroscopy) can be used to characterize the assembly of biological molecules at surfaces in atom- and orbital-specific fashion. To illustrate the range of applications, we begin with simple self-assembled monolayers (SAMs), proceed to SAMs with customized terminal groups, and finish with DNA oligonucleotides and Ribonuclease A, a small protein containing 124 amino acids. The N 1s absorption edge is particularly useful for characterizing DNA and proteins because it selectively interrogates the π* orbitals in nucleobases and the peptide bonds in proteins. Information about the orientation of molecular orbitals is obtained from the polarization dependence. Quantitative NEXAFS models explain the polarization dependence in terms of molecular orientation and structure.Key words: NEXAFS, bio-interfaces, ribonuclease A, immobilization, orientation.

scholarly journals In Vitro and Cellular Self-Assembly of a Zn-Binding Protein Cryptand via Templated Disulfide Bonds

2013 ◽  
Vol 135 (32) ◽  
pp. 12013-12022 ◽  
Author(s):  
Annette Medina-Morales ◽  
Alfredo Perez ◽  
Jeffrey D. Brodin ◽  
F. Akif Tezcan
Keyword(s):  
Self Assembly ◽  
Disulfide Bonds ◽  
Binding Protein

scholarly journals Quantitative Disassembly and Reassembly of Human Papillomavirus Type 11 Viruslike Particles In Vitro

1998 ◽  
Vol 72 (1) ◽  
pp. 32-41 ◽  
Author(s):  
Michael P. McCarthy ◽  
Wendy I. White ◽  
Frances Palmer-Hill ◽  
Scott Koenig ◽  
Joann A. Suzich
Keyword(s):  
Human Papillomavirus ◽  
Ionic Strength ◽  
Self Assembly ◽  
Disulfide Bonds ◽  
Structural Protein ◽  
Homogeneous Population ◽  
Carbonate Buffer ◽  
Viruslike Particles

ABSTRACT The human papillomavirus (HPV) capsid is primarily composed of a structural protein denoted L1, which forms both pentameric capsomeres and capsids composed of 72 capsomeres. The L1 protein alone is capable of self-assembly in vivo into capsidlike structures referred to as viruslike particles (VLPs). We have determined conditions for the quantitative disassembly of purified HPV-11 L1 VLPs to the level of capsomeres, demonstrating that disulfide bonds alone are essential to maintaining long-term HPV-11 L1 VLP structure at physiological ionic strength. The ionic strength of the disassembly reaction was also important, as increased NaCl concentrations inhibited disassembly. Conversely, chelation of cations had no effect on disassembly. Quantitative reassembly to a homogeneous population of 55-nm, 150S VLPs was reliably achieved by the re-formation of disulfide linkages following removal of reducing agent at near-neutral pH and moderate NaCl concentration. HPV-11 L1 VLPs could also be dissociated by treatment with carbonate buffer at pH 9.6, but VLPs could not be regenerated following carbonate treatment. When probed with conformationally sensitive and/or neutralizing monoclonal antibodies, both capsomeres generated by disulfide reduction of purified VLPs and reassembled VLPs formed from capsomeres upon removal of reducing agents exhibited epitopes found on the surface of authentic HPV-11 virions. Antisera raised against either purified VLP starting material or reassembled VLPs similarly neutralized infectious HPV-11 virions. The ability to disassemble and reassemble VLPs in vitro and in bulk allows basic features of capsid assembly to be studied and also opens the possibility of packaging selected exogenous compounds within the reassembled VLPs.

scholarly journals Thiophosphopeptides Instantly Targeting Golgi Apparatus and Selectively Killing Cancer Cells

2021 ◽  
Author(s):  
Weiyi Tan ◽  
Qiuxin Zhang ◽  
Jiaqing Wang ◽  
Meihui Yi ◽  
Hongjian He ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Golgi Apparatus ◽  
Oxygen Atom ◽  
Cancer Cells ◽  
Self Assembly ◽  
Disulfide Bonds ◽  
Unexpected Result ◽  
Subcellular Compartment ◽  
Self Assembling ◽  
Order Of Magnitude

ABSTRACTGolgi apparatus is emerging as a key signaling hub of cells, but there are few approaches for targeting Golgi and selectively killing cancer cells. Here we show an unexpected result that changing an oxygen atom of the phosphoester bond in phospho-peptides by a sulfur atom enables instantly targeting Golgi apparatus (GA) and selectively killing cancer cells by enzymatic self-assembly. Specifically, conjugating cysteamine S-phosphate to the C-terminal of a self-assembling peptide generates a thiophospho-peptide. Being a substrate of alkaline phosphatase (ALP), the thiophosphopeptide undergoes rapid ALP-catalyzed dephosphorylation to form a thiopeptide that self-assembles. The thiophosphopeptide enters cells via caveolin-mediated endocytosis and macropinocytosis and instantly accumulates in GA because of dephosphorylation and formation of disulfide bonds in Golgi. Moreover, the thiophosphopeptide, targeting Golgi, potently and selectively inhibits cancer cells (e.g., HeLa) with the IC50 (about 3 μM), which is an order of magnitude more potent than that of the parent phosphopeptide. This work, as the first report of thiophospho-peptide for targeting Golgi, illustrates a new molecular platform for designing enzyme responsive molecules that target subcellular compartment for functions.

Regeneration Studies of an Analog of Ribonuclease A Missing Disulfide Bonds 65−72 and 40−95†

Biochemistry ◽  
1997 ◽  
Vol 36 (42) ◽  
pp. 13068-13076 ◽  
Author(s):  
Cathy C. Lester ◽  
Xiaobing Xu ◽  
John H. Laity ◽  
Sakurako Shimotakahara ◽  
Harold A. Scheraga
Keyword(s):  
Disulfide Bonds ◽  
Ribonuclease A
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