Relevant bibliographies by topics / Constrained peptides

Academic literature on the topic 'Constrained peptides'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Constrained peptides"

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Bozovičar, Krištof, and Tomaž Bratkovič. "Small and Simple, yet Sturdy: Conformationally Constrained Peptides with Remarkable Properties." International Journal of Molecular Sciences 22, no. 4 (February 5, 2021): 1611. http://dx.doi.org/10.3390/ijms22041611.

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The sheer size and vast chemical space (i.e., diverse repertoire and spatial distribution of functional groups) underlie peptides’ ability to engage in specific interactions with targets of various structures. However, the inherent flexibility of the peptide chain negatively affects binding affinity and metabolic stability, thereby severely limiting the use of peptides as medicines. Imposing conformational constraints to the peptide chain offers to solve these problems but typically requires laborious structure optimization. Alternatively, libraries of constrained peptides with randomized modules can be screened for specific functions. Here, we present the properties of conformationally constrained peptides and review rigidification chemistries/strategies, as well as synthetic and enzymatic methods of producing macrocyclic peptides. Furthermore, we discuss the in vitro molecular evolution methods for the development of constrained peptides with pre-defined functions. Finally, we briefly present applications of selected constrained peptides to illustrate their exceptional properties as drug candidates, molecular recognition probes, and minimalist catalysts.
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Deschamps, J. R., C. George, C. Moore, R. Cudney, and J. L. Flippen-Anderson. "Constrained linear opioid peptides." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C249. http://dx.doi.org/10.1107/s0108767396089489.

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Bode, S. A., and D. W. P. M. Löwik. "Constrained cell penetrating peptides." Drug Discovery Today: Technologies 26 (December 2017): 33–42. http://dx.doi.org/10.1016/j.ddtec.2017.11.005.

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Yin, Hang. "Constrained Peptides as Miniature Protein Structures." ISRN Biochemistry 2012 (September 26, 2012): 1–15. http://dx.doi.org/10.5402/2012/692190.

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This paper discusses the recent developments of protein engineering using both covalent and noncovalent bonds to constrain peptides, forcing them into designed protein secondary structures. These constrained peptides subsequently can be used as peptidomimetics for biological functions such as regulations of protein-protein interactions.
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Moll, Gert N., Anneke Kuipers, Rick Rink, Tjibbe Bosma, Louwe de Vries, and Pawel Namsolleck. "Biosynthesis of lanthionine-constrained agonists of G protein-coupled receptors." Biochemical Society Transactions 48, no. 5 (October 14, 2020): 2195–203. http://dx.doi.org/10.1042/bst20200427.

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The conformation with which natural agonistic peptides interact with G protein-coupled receptor(s) (GPCR(s)) partly results from intramolecular interactions such as hydrogen bridges or is induced by ligand–receptor interactions. The conformational freedom of a peptide can be constrained by intramolecular cross-links. Conformational constraints enhance the receptor specificity, may lead to biased activity and confer proteolytic resistance to peptidic GPCR agonists. Chemical synthesis allows to introduce a variety of cross-links into a peptide and is suitable for bulk production of relatively simple lead peptides. Lanthionines are thioether bridged alanines of which the two alanines can be introduced at different distances in chosen positions in a peptide. Thioether bridges are much more stable than disulfide bridges. Biosynthesis of lanthionine-constrained peptides exploiting engineered Gram-positive or Gram-negative bacteria that contain lanthionine-introducing enzymes constitutes a convenient method for discovery of lanthionine-stabilized GPCR agonists. The presence of an N-terminal leader peptide enables dehydratases to dehydrate serines and threonines in the peptide of interest after which a cyclase can couple the formed dehydroamino acids to cysteines forming (methyl)lanthionines. The leader peptide also guides the export of the formed lanthionine-containing precursor peptide out of Gram-positive bacteria via a lanthipeptide transporter. An engineered cleavage site in the C-terminus of the leader peptide allows to cleave off the leader peptide yielding the modified peptide of interest. Lanthipeptide GPCR agonists are an emerging class of therapeutics of which a few examples have demonstrated high efficacy in animal models of a variety of diseases. One lanthipeptide GPCR agonist has successfully passed clinical Phase Ia.
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Real, Eléonore, Jean-Christophe Rain, Véronique Battaglia, Corinne Jallet, Pierre Perrin, Noël Tordo, Peggy Chrisment, Jacques D'Alayer, Pierre Legrain, and Yves Jacob. "Antiviral Drug Discovery Strategy Using Combinatorial Libraries of Structurally Constrained Peptides." Journal of Virology 78, no. 14 (July 15, 2004): 7410–17. http://dx.doi.org/10.1128/jvi.78.14.7410-7417.2004.

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ABSTRACT We have developed a new strategy for antiviral peptide discovery by using lyssaviruses (rabies virus and rabies-related viruses) as models. Based on the mimicry of natural bioactive peptides, two genetically encoded combinatorial peptide libraries composed of intrinsically constrained peptides (coactamers) were designed. Proteomic knowledge concerning the functional network of interactions in the lyssavirus transcription-replication complex highlights the phosphoprotein (P) as a prime target for inhibitors of viral replication. We present an integrated, sequential drug discovery process for selection of peptides with antiviral activity directed against the P. Our approach combines (i) an exhaustive two-hybrid selection of peptides binding two phylogenetically divergent lyssavirus P's, (ii) a functional analysis of protein interaction inhibition in a viral reverse genetic assay, coupled with a physical analysis of viral nucleoprotein-P complex by protein chip mass spectrometry, and (iii) an assay for inhibition of lyssavirus infection in mammalian cells. The validity of this strategy was demonstrated by the identification of four peptides exhibiting an efficient antiviral activity. Our work highlights the importance of P as a target in anti-rabies virus drug discovery. Furthermore, the screening strategy and the coactamer libraries presented in this report could be considered, respectively, a general target validation strategy and a potential source of biologically active peptides which could also help to design pharmacologically active peptide-mimicking molecules. The strategy described here is easily applicable to other pathogens.
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Kuepper, Arne, Niall M. McLoughlin, Saskia Neubacher, Alejandro Yeste-Vázquez, Estel Collado Camps, Chandran Nithin, Sunandan Mukherjee, et al. "Constrained peptides mimic a viral suppressor of RNA silencing." Nucleic Acids Research 49, no. 22 (December 6, 2021): 12622–33. http://dx.doi.org/10.1093/nar/gkab1149.

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Abstract The design of high-affinity, RNA-binding ligands has proven very challenging. This is due to the unique structural properties of RNA, often characterized by polar surfaces and high flexibility. In addition, the frequent lack of well-defined binding pockets complicates the development of small molecule binders. This has triggered the search for alternative scaffolds of intermediate size. Among these, peptide-derived molecules represent appealing entities as they can mimic structural features also present in RNA-binding proteins. However, the application of peptidic RNA-targeting ligands is hampered by a lack of design principles and their inherently low bio-stability. Here, the structure-based design of constrained α-helical peptides derived from the viral suppressor of RNA silencing, TAV2b, is described. We observe that the introduction of two inter-side chain crosslinks provides peptides with increased α-helicity and protease stability. One of these modified peptides (B3) shows high affinity for double-stranded RNA structures including a palindromic siRNA as well as microRNA-21 and its precursor pre-miR-21. Notably, B3 binding to pre-miR-21 inhibits Dicer processing in a biochemical assay. As a further characteristic this peptide also exhibits cellular entry. Our findings show that constrained peptides can efficiently mimic RNA-binding proteins rendering them potentially useful for the design of bioactive RNA-targeting ligands.
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Corr, M., L. F. Boyd, S. R. Frankel, S. Kozlowski, E. A. Padlan, and D. H. Margulies. "Endogenous peptides of a soluble major histocompatibility complex class I molecule, H-2Lds: sequence motif, quantitative binding, and molecular modeling of the complex." Journal of Experimental Medicine 176, no. 6 (December 1, 1992): 1681–92. http://dx.doi.org/10.1084/jem.176.6.1681.

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To gain insight into the rules that govern the binding of endogenous and viral peptides to a given major histocompatibility complex (MHC) class I molecule, we characterized the amino acid sequences of a set of self peptides bound by a soluble analogue of murine H-2Ld, H-2Lds. We tested corresponding synthetic peptides quantitatively for binding in several different assays, and built three-dimensional computer models of eight peptide/H-2Lds complexes, based on the crystallographic structure of the human HLA-B27/peptide complex. Comparison of primary and tertiary structures of bound self and antigenic peptides revealed that residues 2 and 9 were not only restricted in sequence and tolerant of conservative substitutions, but were spatially constrained in the three-dimensional models. The degree of sequence variability of specific residues in MHC-restricted peptides reflected the lack of structural constraint on those amino acids. Thus, amino acid residues that define a peptide motif represent side chains required or preferred for a close fit with the MHC class I heavy chain.
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Willick, Gordon, Paul Morley, and James Whitfield. "Constrained Analogs of Osteogenic Peptides." Current Medicinal Chemistry 11, no. 21 (November 1, 2004): 2867–81. http://dx.doi.org/10.2174/0929867043364153.

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Ladner, Robert C. "Constrained peptides as binding entities." Trends in Biotechnology 13, no. 10 (October 1995): 426–30. http://dx.doi.org/10.1016/s0167-7799(00)88997-0.

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Dissertations / Theses on the topic "Constrained peptides"

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Shi, Feng, and 石峰. "Synthesis, characterization and application of constrained 7/8 helix." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2010. http://hub.hku.hk/bib/B44363229.

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In this thesis, constrained 7/8 helix has been developed to enhance the stability of 7/8 helical structure in polar and aqueous solvents for biological application. The synthesis of constrained 7/8 helical peptides has been achieved in two steps. In the first step, a 7/8 helical peptide chain comprising alternating α-L-amino acids and α-D-aminoxy acids was assembled by standard solution phase peptide synthesis protocol. In the second step, a covalent cross-linker as the conformational constraint was incorporated into 7/8 helical peptide at adjacent α-amino acid residues by consecutive intramolecular ring-closing olefin metathesis reaction and catalytic hydrogenation reaction. Conformational properties of constrained 7/8 helical peptides have been explored by applying NMR spectroscopy, theoretical calculation, and circular dichroism spectroscopy to three constrained tetrapeptides 2.2–2.4 and one non-cross-linked reference peptide 2.1. It was discovered that constrained 7/8 helical peptides with a saturated methylene chain as the covalent cross-linker maintained the structural feature of alternating N–O turns and γ-turns, and exhibited increased stability in both organic solvents and aqueous media. No obvious difference was observed for the covalent cross-linker with six, seven, or eight methylene units in improving the stability of 7/8 helix. The constrained 7/8 helix with enhanced structural stability was applied in the design of α-helix mimics. Based on the structure of helix D in the crystal structure of CD81 large extracellular loop, the putative receptor of Hepatitis C Virus envelop 2 (HCV E2) protein, constrained 7/8 helical hexapeptides 4.1 and 4.2 with free N-terminus were designed and synthesized in the form of TFA salt as the candidates of helix D mimics. It was expected that peptides 4.1 and 4.2 could act as the inhibitors of the interaction between helix D and HCV E2 to block HCV entry into cells. Unfortunately, the biological activity test on the ability of peptides 4.1 and 4.2 in HCV inhibition revealed that none of these peptides exhibited detectable inhibitory effect on the entry of HCV into cells and HCV replication at the concentration of 100 μM.
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Chemistry
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Doctor of Philosophy
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Pugh, Darren Charles. "The synthesis of conformationally constrained peptides and novel assymetric catalysts." Thesis, King's College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.401641.

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Anderson, Kelly Helen. "The Synthesis and Surface Studies of β-Amino Acids & β-Peptides." Thesis, University of Canterbury. Chemistry, 2007. http://hdl.handle.net/10092/1441.

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This thesis examines the synthesis of conformationally constrained β-amino acids and β- peptides, and the electron transfer properties of the latter when immobilised on gold. Additionally, cross metathesis on gold was investigated as a method for surface functionalisation. Chapter One introduces the concepts of electron transfer in nature, how it is facilitated by the secondary structure in α-peptides, and why β-peptides might be useful for studying electron transfer. This is followed by a discussion of the properties of β-peptides, including the enhanced stability and variety of helical secondary structures and the greater potential for functionalisation of the peptide backbone when compared to α-peptides. Finally, the conformational constraints of ring-systems on cyclic amino acids is discussed, with reference to the stabilising effect of these compounds on peptide secondary structures. Chapter Two describes the electrochemical analysis of β-hexapeptides immobilised on gold. The chapter is prefaced by a discussion of the important electron transfer mechanisms for peptides, the fabrication of peptide-gold self-assembled monolayer (SAM) interfaces, and the electron transfer in helical α-peptides. β-Peptides containing an electroactive ferrocene moeity were immobilised on gold and studied using cyclic voltammetry and chronoamperometry. The latter method was used to examine the dependence of the electron transfer rate on overpotential, thereby determining the likely mode of electron transfer through the β-peptides SSβ₆Fc, Fcβ₆SS and SC₁₅β₆Fc. These peptides exhibited very weak dependence on overpotential, characteristic of electron transfer behaviour of an electron hopping mechanism (which is also thought to occur in helical α-peptides). Both the dipole moment of the peptides and the structure of the sulfurlinker group were found to be important in determining the rate of electron transfer. Conversely, the equivalent α-peptide SSα₆Fc exhibited electron transfer behaviour characteristic of the less efficient tunnelling mechanism, which is thought to operate in strand-like peptides. Chapter Three examines the application of cross metathesis, using a Grubbs' second generation catalyst, as a means to functionalise olefin-terminated self-assembled monolayers on gold. Abstract iv Firstly, an introduction into the limited published research on cross metathesis on both planar surfaces and nanoparticles is given. Olefin-terminated thiol 3.18, suitable for immobilisation on gold, and solution phase olefin-terminated ferrocene 3.10 were synthesised as reactants for cross metathesis studies. An analytical methodology was developed involving the cross metathesis of surface-immobilised 3.18 with ferrocene 3.10 in dichloromethane, whereby the concentration of electroactive cross metathesis product 3.22 was monitored electrochemically as a function of time. The concentration of surface-immobilised product 3.22 was determined by integration of the oxidation peak area and found to be highly dependent on both the concentration of immobilised olefin reactant 3.18 and reaction time. Furthermore, the surface concentration of ferrocenyl model disulfide 3.21 and thiol 2.18 decayed markedly upon addition of Grubb's catalyst, as revealed by the decrease in the oxidation peak area, which suggested that catalystmediated desorption was occurring. Chapter Four details the solution-phase synthesis of ferrocene- and thiol-functionalised β- hexapeptides used in both the electron transfer studies described in chapter two, and in the determination of secondary structure using circular dichroism and NMR techniques. The synthesis of simple model compounds 4.14, 4.16 and 4.18 established the incompatibility of the deprotection of methyl and benzyl ester protecting groups with protected-thiol and disulfide linkers, leading to the use of N-hydroxysuccinmide-activated sulfur-linkers 4.20 and 4.22 in further synthesis. A number of β-hexapeptides were synthesised by amide coupling of β- tripeptides functionalised at the N- and C-termini. Structural studies of the methanol soluble β- hexapeptide 4.60 suggested that the covalent attachment of ferrocene moeity to the C-terminus of a β-peptide did not disrupt the formation of a 14-helix in solution. β-peptides containing functionality at both the C- and N-termini (such as SSβ₆Fc, SSβ₆Et and acetyl-protected SC₁₅β₆Fc) were not suitable for solution phase structural studies; however, molecular modelling suggested that helical conformations are the most stable these β-peptides in solution phase. Chapter Five outlines the synthesis of novel cyclic β-amino acids by two different general synthetic routes. The first uses an efficient conjugate addition/fluorination reaction of α,β- unsaturated esters with lithiated chiral secondary amines to prepare the novel cyclopentyl- and cyclohexyl-based fluorinated β-amino acids 2.43a and 2.43b. The high diastereoselectivity of this reaction, which introduces two stereocentres into the achiral unsaturated esters, is directed by the configuration of the attacking amine. The second methodology utilizes the versatile ringclosing metathesis reaction in the synthesis of novel cyclic β-amino acids. A stereoselective Abstract v trans-alkylation of olefinic β-amino acids gave the required β-dienes 5.62 and 5.77. Optimised cyclisation yields were achieved with a Grubb's 2nd generation catalyst for diene 5.62 and Grubb's 1st generation catalyst for diene 5.77, to give the trans-cycloheptyl- and cyclooctylbased β-amino acids 5.63 and 5.78, respectively. The attempted synthesis of cyclononyl-based β-amino acid 5.87 using both catalysts yielded only cyclic dimer products 5.88 and 5.89. The trans configuration of the 5.62 diene was confirmed by x-ray crystallography. Chapter Six is an experimental chapter and outlines the electrochemical setup and analysis, and the synthesis, purification and characterisation of compounds described in this thesis.
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Chen, Kuangyu. "Intracellular Protein Delivery by Genetically Encoded and Structurally Constrained Cell-Penetrating Peptides." The Ohio State University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1555628591555136.

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Davidson, James Prentice. "Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide mimics /." Full text (PDF) from UMI/Dissertation Abstracts International, 2001. http://wwwlib.umi.com/cr/utexas/fullcit?p3008309.

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Aguesseau, Julie. "Design of bio-inspired catalysts based on a gamma-peptide foldamer architecture." Thesis, Montpellier, 2019. http://www.theses.fr/2019MONTS043/document.

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Les travaux décrits dans ce manuscrit concernent la synthèse d’oligomères de γ-amino acides hétérocycliques contraints, appelés ATCs (acides 4-Amino-(méthyl)-1,3-Thiazole-5-Carboxyliques), leur application en catalyse énamine et leur étude structurale. Les monomères d’ATC sont construits autour d’un noyau thiazole inséré entre les carbones Cα-Cβ, permettant de limiter la valeur de l’angle dièdre ζ à 0°. La présence de deux points de substitution, sur le carbone γ asymétrique et en position 2 du noyau aromatique, permet une large diversification structurale des ATCs. Ainsi, plusieurs séries d’oligomères ont été synthétisées par couplages peptidiques sur support solide. Une étude structurale de ces oligomères par RMN, IR-TF, cristallographie RX et dichroïsme circulaire a démontré qu’ils adoptaient une structure en helice C9, résultant d’un réseau de liaisons hydrogène de type COi---NHi+2 s’établissant tout au long de la séquence. L’objectif du projet présenté ici vise à étudier l’impact de la conformation des architectures développées, à la fois sur la sélectivité et sur l’induction asymétrique dans la réaction de nitro-Michael pour trois réactifs différents. Le dernier axe de ce travail a été de développer une méthode de modélisation sous contraintes RMN spécifique à la génération de modèles tridimentionel d’oligomères d’ATCs
The work described in this manuscript is devoted to the synthesis of heterocyclic constrained γ-amino acids, named ATCs (4-Amino-(methyl)-1,3-Thiazole-5-Carboxylic acids), their application in enamine catalysis and their structural study. ATC monomers are built around a thiazole ring providing a conformational limitation around the Cα and Cβ at 0°. The presence of two diversification points both on the γ asymmetric carbon and on the position 2 of the aromatic ring, allows a large structural diversification of the ATCs. Therefore, several oligomers were synthesized using solid phase peptide synthesis. A structural study of these oligomers, employing NMR, FTIR, circular dichroism and crystallography RX, demonstrated that they adopt a C9-right-handed helix stabilized by a hydrogen bond pattern between COi---NHi+2 along the helix. The objective of the project presented in this manuscript was the design and the structural characterization of molecular edifices with predictable folding properties and the systematic study of structure-function relationships in the nitro-Michael addition reaction, for three different substrates. Eventually, the last part of this work focused on the development of a new methodology, specific to ATC-oligomers, to perform 3D-modelling studies using NMR refinement
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Cai, Chaozhong. "Asymmetric synthesis of chi-constrained pyroglutamic acids, glutamic acids and prolines for peptides and peptidomimetics." Diss., The University of Arizona, 2001. http://hdl.handle.net/10150/280129.

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The recent upsurge of interest in the peptide-based drug molecules has been accompanied by a great deal of attention to the design of stereochemically defined non-proteinogenic amino acids. As a continuous effort to develop efficient syntheses of χ-constrained amino acids in our group, we recently have developed a practical methodology for the asymmetric synthesis of substituted pyroglutamic acid, glutamic acid and proline analogues, which are of important use in examining the relationships between conformation and bioactivities of biologically important peptides (e.g. DPDPE, α-MSH). The key step in this method is an asymmetric Michael addition reaction between a chiral Ni(II)-complex of the glycine Schiff base (S)-NiGlyBPB, and derivatives of α,β-unsaturated carboxylic acids. This new method is the first highly diastereoselective, room temperature, organic base-catalyzed, asymmetric Michael addition reaction. Excellent chemical yields and diastereoselectivity, along with the simplicity of experimental procedure, renders the present method of immediate use for preparation of various novel beta-substituted pyroglutamic acids, glutamic acids and prolines. Decomposing the resulting addition products in acidic medium, followed by neutralizing with ammonia, gave optically pure substituted pyroglutamic; acids in good yields (>80%). The substituted pyroglutamic acids were converted to the corresponding substituted glutamic acids by hydrolysis in 6N HCl, or to substituted proline analogues by selective reduction of amide carbonyl group to a methylene group. Both novel substituted glutamic acids and prolines are being incorporated into biologically important peptide MT-II analogues for structure-activity studies.
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Palmer, Simon James. "A technique for constructing a DNA library encoding a structurally diverse repertoire of constrained peptides." Thesis, University of Bath, 1998. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267346.

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Vasco, Vidal Aldrin [Verfasser], Ludger [Gutachter] Wessjohann, and Daniel G. [Gutachter] Rivera. "Multicomponent cyclization strategies to novel conformationally constrained peptides / Aldrin Vasco Vidal ; Gutachter: Ludger Wessjohann, Daniel G. Rivera." Halle (Saale) : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2020. http://d-nb.info/121073172X/34.

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Spanopoulou, Anna [Verfasser], Aphrodite [Akademischer Betreuer] Kapurniotu, Horst [Gutachter] Kessler, and Aphrodite [Gutachter] Kapurniotu. "Synthesis and study of conformationally constrained peptides as inhibitors of amyloid self-assembly / Anna Spanopoulou ; Gutachter: Horst Kessler, Aphrodite Kapurniotu ; Betreuer: Aphrodite Kapurniotu." München : Universitätsbibliothek der TU München, 2019. http://d-nb.info/1213025869/34.

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Books on the topic "Constrained peptides"

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Arttamangkul, Seksiri. Synthesis and opioid activity of conformationally constrained dynorphin A analogues. 1995.

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Book chapters on the topic "Constrained peptides"

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Ede, N. J., N. Lim, I. D. Rae, I. Cosic, F. M. Ng, M. I. Aguilar, and M. T. W. Hearn. "Conformationally constrained peptide analogs with hypoglycaemic activity." In Peptides, 268–70. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_95.

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Genin, Michael J., Uma Sreenivasan, and Rodney L. Johnson. "Conformationally constrained analogs of L-prolyl-L-leucylglycinamide." In Peptides, 757–58. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_304.

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Kanmera, T., A. Mori, T. Minegishi, and Y. Nakao. "Conformationally constrained PTH-related protein antagonists." In Peptides 1994, 650–51. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_297.

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Rockway, T. W., E. T. Olejniczak, E. M. Devine, G. P. Budzik, T. J. Opgenorth, and W. H. Holleman. "Conformationally constrained peptide analogs of atrial natriuretic factor (ANF)." In Peptides, 249–51. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-010-9060-5_80.

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Fassina, G., P. Scardino, M. Ruvo, P. Fucile, P. Amodeo, and G. Cassani. "Synthesis of conformationally constrained dimeric peptide libraries." In Peptides 1994, 489–90. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_221.

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Pons, Jean-François, Mamadou Sow, Frédéric Lamaty, Jean-Luc Fauchére, Annie Molla, Philippe Viallefont, and René Lazaro. "New RGD amphiphilic cyclic peptide and new RGD-mimetic constrained diketopiperazines." In Peptides Frontiers of Peptide Science, 176–77. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x_69.

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Garvey, David S., Paul D. May, and Alex M. Nadzan. "Synthesis of conformationally constrained CCK-4 analogs containing a substituted gamma lactam ring." In Peptides, 123–25. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_36.

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Danho, W., J. Tilley, S. J. Shiuey, I. Kulesha, J. Swistok, R. Makofske, J. Michalewsky, et al. "Conformationally constrained analogs of CCK-7 with anorexic activity." In Peptides 1992, 149–51. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_54.

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Morgan, Barry A., Jasbir Singh, Eugene Baizman, Harry Bentley, Doriann Keifer, and Susan Ward. "Structure-function studies in a series of tachykinin antagonists containing a conformationally constrained tryptophan analog." In Peptides, 508–9. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_152.

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Lin, Ying, Dev Trivedi, Mara Siegel, and Victor J. Hruby. "Conformationally constrained glucagon analogs: New evidence for the conformational features important to glucagon-receptor interactions." In Peptides, 439–40. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_165.

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Conference papers on the topic "Constrained peptides"

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Blodgett, Karl, and Timothy Zwier. "JET-COOLED, CONFORMER-SPECIFIC IR SPECTRA OF CYCLICALLY-CONSTRAINED _-PEPTIDES. DOES CONDENSED PHASE STRUCTURE SURVIVE THE VACUUM?" In 74th International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2019. http://dx.doi.org/10.15278/isms.2019.tj10.

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Lasota, Anika, Oliwia Fraczak, Adriana Muchowska, Aleksandra Misicka, Michal Nowakowski, Maciej Maciejczyk, Andrzej Ejchart, and Aleksandra Olma. "Structure-Activity Relationships of Constrained Dermorphin Analogues Containing an α-Alkyl-β-Substituted Alanines." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.073.

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Van Den Hauwe, Robin, Olivier Van der Poorten, Steven Ballet, Emilie Eiselt, Phillipe Sarret, Louis Gendron, and Dirk Tourwé. "1,5-Benzothiazepinone and arylazepinone dipeptide mimetics as local constraints in peptidomimetic design." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.178.

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Haghighi, Saghar Mowlazadeh, Minying Cai, Yang Zhou, Bailey Lahtinen, and Victor J. Hruby. "Conformationally Constrained Ac-His-D-Nal(2’)-Nle-Trp-NH2 Analogues Leads to Selective Melanotropins." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.189.

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Bodero, Lizeth, Gregory Chaume, Nathalie Lensen, Karine Guitot, Sandrine Ongeri, Olivier Lequin, and Thierry Brigaud. "Control, Quantification and Assignment of Screw-Sense Preference in Helical Aib Foldamers by Introducing the Chiral Constrained α-Trifluoromethylalanine." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.298.

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Caoili, Salvador Eugenio C. "Development of a Polymer-Theoretic Approach to Describing Constraints on Reactions Between Antipeptide Antibodies and Intrinsically Disordered Peptide Antigens." In BCB '17: 8th ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics. New York, NY, USA: ACM, 2017. http://dx.doi.org/10.1145/3107411.3108190.

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Tran, Phat L., Jessica R. Gamboa, Katherine E. McCracken, Jeong-Yeol Yoon, and Marvin J. Slepian. "Interaction With Nanoscale Topography: The Use of Nanowell-Trapped Charged Ligand-Bearing Nanoparticle Surfaces To Modulate Physiological Focal Adhesions in Endothelial Cells." In ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/nemb2013-93345.

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Abstract:
Achieving cell adhesion, growth and homeostasis on an underlying biomaterial surface may be a desirable feature in implant device design and tissue engineering. Insight has been gained from numerous cell patterning strategies where spatial cues and physical constraints have been shown to regulate the structure and function of cells. Despite significant advances in modifying substrates for cellular attachment, migration and proliferation, the achievement of confluent and aligned growth of functional endothelial cells on cardiovascular blood-contacting implants under physiologically significant wall shear stress has proven difficult. Recently we have reported on a method that enhances cellular adhesion under flow conditions on synthetic polymer surfaces, without reliance on pro-adhesive protein biomaterials, which are often thrombogenic. In this method we utilize electron beam lithography and size-dependent self-assembly to fabricate line arrays of nanowells allowing entrapment and retention of charged nanoparticles, covalently conjugated with a RGD adhesive ligand, GRGDSPK. This approach is an additive strategy of combining substrata topographic alteration, electrostatic charge and biochemical ligands, all uniquely incorporated as an ensemble of charged, ligand-bearing nanoparticles entrapped in arrays of nanowells. However, the modulation of endothelial cell physiologic mechanisms as a result of ensemble surface exposure remains to be characterized. In this report, we extend our studies and probe cell physiologic mechanisms altered as a result of nanofeatured surface exposure. We first examined the functional intactness or normalcy of endothelial cells adherent to the nanofeatured ensemble surface utilizing standard immunostaining and flow cytometry methods. We found β1-integrin expression dominated quiescent adherent endothelial cells while αVβ3-integrins expression was more common in migratory cells. Endothelial cells were noted to express high levels of PECAM-1 over time when exposed to nanofeatured surface and RGD peptides. For understanding the contribution of the nanofeatured surface (entrapped RGD conjugated nanoparticles) to cell adhesion, cytochalasin B was used to alter cell spreading. Confocal microscopy illustrated the uptake of nanoparticles in endothelial cells on composite surfaces, as well as the inhibition of this endocytosis by cytochalasin B. After prohibiting the cells from engulfing nanoparticles, we found an 80% reduction in cell adhesion; suggesting that an endocytic mechanism might play a role in maintaining cell adhesion. Nanofeatured ensemble surfaces appear to be good substrates for achieving a high level of EC adhesion, with maintained growth and stability.
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