MHC-peptide/TCR complexes

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Sandy's picture
MHC-peptide/TCR complexes

Antigen recognition, internalization and expression as peptide by MHC class I and class II is fascinating.

What are the methods to study mimic recognition processes and membrane interfaces? I mean surface sensitive techniques.

Roshan's picture
Sandy wrote:Antigen

Sandy wrote:

Antigen recognition, internalization and expression as peptide by MHC class I and class II is fascinating.

What are the methods to study mimic recognition processes and membrane interfaces? I mean surface sensitive techniques.

found these information on the internet:

Our research group aims at understanding the surface chemistry, spectroscopic and microscopic investigation of organic and biological supramolecular complexes. The chemistry of monolayers of supramolecular complexes is of paramount importance on account of many potential applications in diverse fields such as manufacture of new polymers, bio- and chemisensors, protective surface coatings, conductive films, optoelectronic devices, etc.

Specifically we are focusing on:

Combinatorial chemistry

Molecular recognition

Development of chemi- and biosensors

Tissue engineering

Aggregation studies regarding amyloidogenesis

I. Combinatorial chemistry

We are exploring the novel idea of using 2D combinatorial chemistry methodology to recognize toxin molecules, to catalyze special reactions, and to mimic function of enzymes.

peptide linker hydrophobic tail

By a combination of different peptide length, sequence and linker, we are interested in screening the amphiphilic peptide lipids library to discover the leading amphiphilic lipids with the best binding affinity or the best catalytic effect to mimic enzymes.

II. Molecular recognition

The molecular recognition process at biomembrane interfaces plays a crucial role in biological systems. Another long-term objective of our group is to understand the molecular interaction and recognition phenomenon at air/water interface. Specifically, we are studying the interactions between enzymes (OPAA, OPH) and organophosphorus compounds in monolayers. This project funded by a federal agency ultimately aims at developing a sensitive biosensor using enzyme monolayers for the detection of traces of pesticides in aqueous solutions. The detection method is based on photonics.

III. Development of chemi- and biosensors

The long term goal of this project is to develop an optical fiber sensing device to detect the presence of toxins (marine toxin) by fluorescence emission. The major goals are: i) to optimize fluorescence response and selectivity of a chemical sensor to a toxin through molecular recognition , ii) to prepare a sensor derivative and incorporate into an organized assembly such as a monolayer at air/water interface and evaluate the response in 2D array, and iii) to synthesize a molecular sensor suitable for covalent attachment and study the response to toxins.

IV. Tissue engineering

Photocrosslinking provides an effective and benign method for in situ gelation. Facile photogelation exhibits considerable advantages lacked by conventional chemical methods. We are preparing hydrophilic polymers such as PEG, dextran, chitosan macromers with photosensitive groups such as anthrancene and nitrocinnamate. Our preliminary results show that the synthesized macromers can form hydrogel very quickly upon longwave UV irradiation. Additionally, some of these polymers exhibit photoreversibility . These hydrogels will be highly promising in biotechnical and biomedical applications ranging from controlled drug delivery and enzyme immobilization to size-selective biomembranes and wound healing dressings.

V. Aggregation studies regarding Amyloidogenesis

Amyloidogenesis is a very important factor in developing Alzheimer's Disease (AD). AD is known as a progressive neurodegenerative disease that has been the focus of many research endeavors over the few last decades. AD is known to form the so called amyloid plaque which is formed by extracellular aggregates of protein affecting the brain parenchyma and the neurofibrillary tangles which are intracellular aggregates composed of paired helical filaments of hyperphosphorylated tau protein. Surface chemistry is known to be a biomimetic model that can mimic biological systems. Its methodology can be used to study structure conformations, molecular orientation and membrane diffusion. The advantage of surface chemistry is the use of the air-water interface where the molecules will assemble in a similar way as in a biological membrane. We are proposing a two-dimensional biomimetic approach to the amyloidogenesis. The reason for this approach is that biomimetic studies performed to date are done in solution, but since the cleavage of the -amyloids takes place at a biointerface it seems logical to study the amyloidogenesis in 2-D. Our approach is based on the possibility of designing peptides or peptide libraries that can assemble in protein-like structures or aggregates. We can assemble in the A(1-40) or A(1-42) peptide a fluorescent aminoacid that would enhance contrast in the visualization of the amyloidogenesis by means of intrinsic fluorescence; this would, therefore, not require the addition of octadecanoylamino fluorescein to enhance the contrast.

Selected Publications

Constantine, C.A., S.V. Mello, A. Dupont, X. Cao, D. Santos Jr., O.N. Oliveira Jr., F.T. Stripino, E.C. Pereira, Tu-chen Cheng, J.J. De Franck and R.M. Leblanc. Layer-by-layer self-assembled chitosan poly (thyophene-3-acetic acid) and organophosphorous hydrolase multilayers. J. Am. Chem. Soc. 2003, 125, 1805-1809.

Gattas-Asfura, K.M. and R.M. Leblanc. Peptide coated CdS quantum dots as nanosensors for Cu2+ and Ag+ detection. Chem. Commun. 2003, 2684-2685.

Lauer-Fields, J.L., P. Kele, G. Sui, H. Nagase, R.M. Leblanc and G.B. Fields. Analysis of matrix metalloproteinase triple-helical peptidase activity with substrates incorporating fluorogenic L- or D-aminoacids. Anal. Biochem. 2003, 321, 105-115.

Zheng, Y., X. Cao, J. Orbulescu, V. Konka, F.M. Andreopoulos, Si M. Pham and R.M. Leblanc. Peptidyl fluorescent chemosensors for the detection of divalent copper. Analyt. Chem. 2003, 75, 1706-1712.

Zheng, Y., J. Orbulescu, X. Ji, F.M. Andreopoulos, Si. M. Pham and R.M. Leblanc. Development of fluorescent films sensors for the detection of divalent copper. J. Am. Chem. Soc. 2003, 125, 2680-2686.

Cao, X., G. Sui, Q. Huo and R.M. Leblanc. "Langmuir and Langmuir- Blodgett films of a novel tryptophan peptide lipid". Chem. Commun. 2002, 8/B106 597C, 806-807.

Gawley, R.E., S. Pinet, C.M. Cardona, P.K. Datta, T. Ren, W.C. Guida, J. Nydick and R.M. Leblanc. Chemosensors for the marine toxin saxitoxin. J. Am. Chem. Soc. 2002, 124, 13448-13453.

Zheng, Y., Q. Huo, P. Kele, F.M. Andreopoulos, Si M. Pham and R.M. Leblanc. "A new fluorescent chemosensor for copper ions based on tripeptide Glycyl - Histidyl- Lysine (GHK)". Org. Lett. 2001, 3, 3277-3280.

Huo, Q., S. Russev, T. Hasegawa, J. Nishijo, J. Umemura, G. Puccetti, K.C. Russell and R.M. Leblanc. "A Langmuir monolayer with a nontraditional molecular architecture". J. Am. Chem. Soc., 2000, 122, 7890-7897.

Huo, Q., G. Sui, P. Kele and R.M. Leblanc. "Combinatorial surface chemistry- is it possible?". Angew. Chem. Int. Ed., 2000, 39,1854-1857.

cliff99's picture
To Roshan response I would

To Roshan response I would simply add that some truly excellent structrual work has been done in this area by an old colleague of mine among others. Take a look at:

Wu, et al., (2002) Two-step binding mechanism for T-cell receptor recognition of peptide MHC, Nature, 418:552

Garcia & Adams (2005) How the T cell receptor sees antigen--a structural view, Cell, 122:333 (Review)

Or view the structures directly at - entry 2IAD plus others