Rajkumar Misra

article

Exploring Helical Peptides and Foldamers for the Design of Metal Helix Frameworks: Current Trends and Future Perspectives

Nikhil Bajpayee, Thangavel Vijayakanth, Sigal Rencus‐Lazar, Sneha Dasgupta, more

Flexible and biocompatible metal peptide frameworks (MPFs) derived from short and ultra‐short peptides have been explored for the storage of greenhouse gases, molecular recognition, and chiral transformations. In addition to short flexible peptides, peptides with specifically folded conformations have recently been utilized to fabricate a variety of metal helix frameworks (MHFs). The secondary structures...

article

Exploring Helical Peptides and Foldamers for the Design of Metal Helix Frameworks: Current Trends and Future Perspectives

Nikhil Bajpayee, Thangavel Vijayakanth, Sigal Rencus‐Lazar, Sneha Dasgupta, more

Angewandte Chemie International Edition > 62 > 6 > n/a - n/a

Flexible and biocompatible metal peptide frameworks (MPFs) derived from short and ultra‐short peptides have been explored for the storage of greenhouse gases, molecular recognition, and chiral transformations. In addition to short flexible peptides, peptides with specifically folded conformations have recently been utilized to fabricate a variety of metal helix frameworks (MHFs). The secondary structures...

article

Exploiting Minimalistic Backbone Engineered γ‐Phenylalanine for the Formation of Supramolecular Co‐Polymer

Rajkumar Misra, Yiming Tang, Yujie Chen, Priyadarshi Chakraborty, more

Macromolecular Rapid Communications > 43 > 19 > n/a - n/a

Ordered supramolecular hydrogels assembled by modified aromatic amino acids often exhibit low mechanical rigidity. Aiming to stabilize the hydrogel and understand the impact of conformational freedom and hydrophobicity on the self‐assembly process, two building blocks based on 9‐fluorenyl‐methoxycarbonyl‐phenylalanine (Fmoc‐Phe) gelator which contain two extra methylene units in the backbone, generating...

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From Folding to Assembly: Functional Supramolecular Architectures of Peptides Comprised of Non‐Canonical Amino Acids

Rajkumar Misra, Safra Rudnick‐Glick, Lihi Adler‐Abramovich

Macromolecular Bioscience > 21 > 8 > n/a - n/a

The engineering of biological molecules is the fundamental concept behind the design of complex materials with desirable functions. Over the last few decades, peptides and proteins have emerged as useful building blocks for well‐defined nanostructures with controlled size and dimensions. Short peptides in particular have received much attention due to their inherent biocompatibility, lower synthetic...

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From Folding to Assembly: Functional Supramolecular Architectures of Peptides Comprised of Non‐Canonical Amino Acids

Rajkumar Misra, Safra Rudnick‐Glick, Lihi Adler‐Abramovich

Macromolecular Bioscience > 21 > 8 > n/a - n/a

Front Cover: This review discusses the self‐assembly of various noncoded amino acid‐containing peptides and their applications in nanobiotechnology. The incorporation of non‐coded amino acids in peptide sequences have been shown to form well defined secondary structures, similar to natural proteins, with the ability to self‐assemble and generate a wide variety of nanostructures with excellent biocompatibility...

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Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers

Sanjit Dey, Rajkumar Misra, Abhijith Saseendran, Saikat Pahan, more

Angewandte Chemie International Edition > 60 > 18 > 9863 - 9868

Availing the peptide folded architectures to design metal‐coordinated frameworks and cages is restricted due to the scarcity of readily accessible short and stable secondary structures. The secondary structures, α‐helix and β‐sheets, play significant roles in stabilizing tertiary folds of proteins. Designing such helical structures from the short sequences of peptides without having any steric restrictions...

article

Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers

Sanjit Dey, Rajkumar Misra, Abhijith Saseendran, Saikat Pahan, more

Angewandte Chemie > 133 > 18 > 9951 - 9956

Availing the peptide folded architectures to design metal‐coordinated frameworks and cages is restricted due to the scarcity of readily accessible short and stable secondary structures. The secondary structures, α‐helix and β‐sheets, play significant roles in stabilizing tertiary folds of proteins. Designing such helical structures from the short sequences of peptides without having any steric restrictions...

article

Metal‐Helix Frameworks from Short Hybrid Peptide Foldamers

Rajkumar Misra, Abhijith Saseendran, Sanjit Dey, Hosahudya N. Gopi

Angewandte Chemie International Edition > 58 > 8 > 2251 - 2255

The potential of structured peptides has not been explored much in the design of metal‐organic frameworks (MOFs). This is partly due to the difficulties in obtaining stable secondary structures from the short α‐peptide sequences. Here we report the design, crystal conformations, coordination site dependent different silver coordinated frameworks of short α,γ‐hybrid peptide 12‐helices consisting of...

article

Metal‐Helix Frameworks from Short Hybrid Peptide Foldamers

Rajkumar Misra, Abhijith Saseendran, Sanjit Dey, Hosahudya N. Gopi

Angewandte Chemie > 131 > 8 > 2273 - 2277

The potential of structured peptides has not been explored much in the design of metal‐organic frameworks (MOFs). This is partly due to the difficulties in obtaining stable secondary structures from the short α‐peptide sequences. Here we report the design, crystal conformations, coordination site dependent different silver coordinated frameworks of short α,γ‐hybrid peptide 12‐helices consisting of...

article

Artificial β‐Double Helices from Achiral γ‐Peptides

Rajkumar Misra, Sanjit Dey, Rahi M. Reja, Hosahudya N. Gopi

Angewandte Chemie International Edition > 57 > 4 > 1057 - 1061

Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d‐peptides. In contrast to natural polypeptides, remarkable β‐double‐helical structures from achiral γ‐peptides built from α,β‐unsaturated γ‐amino acids have been observed. The crystal structures suggest that they adopted parallel β‐double helical structures and these structures...

article

Artificial β‐Double Helices from Achiral γ‐Peptides

Rajkumar Misra, Sanjit Dey, Rahi M. Reja, Hosahudya N. Gopi

Angewandte Chemie > 130 > 4 > 1069 - 1073

Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d‐peptides. In contrast to natural polypeptides, remarkable β‐double‐helical structures from achiral γ‐peptides built from α,β‐unsaturated γ‐amino acids have been observed. The crystal structures suggest that they adopted parallel β‐double helical structures and these structures...

article

Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix

Rajkumar Misra, K. Muruga Poopathi Raja, Hans‐Jörg Hofmann, Hosahudya N. Gopi

Chemistry – A European Journal > 23 > 65 > 16644 - 16652

The most important natural α‐ and 3₁₀‐helices are stabilized by unidirectional intramolecular hydrogen bonds along the helical cylinder. In contrast, we report here on 12/10‐helical conformations with alternately changing hydrogen‐bond directionality in sequences of α,γ‐hybrid peptides P1–P5 [P1: Boc‐Ala‐Aic‐Ala‐Aic‐COOH; P2: Boc‐Leu‐Aic‐Leu‐Aic‐OEt; P3: Boc‐Leu‐Aic‐Leu‐Aic‐Leu‐Aic‐Aib‐OMe; P4: Boc‐Ala‐Aic‐Ala‐Aic‐Ala‐Aic‐Ala‐OMe;...

article

Structural Dimorphism of Achiral α,γ‐Hybrid Peptide Foldamers: Coexistence of 12‐ and 15/17‐Helices

Rajkumar Misra, Abhijith Saseendran, Gijo George, Kuruva Veeresh, more

Chemistry – A European Journal > 23 > 15 > 3764 - 3772

Here, novel 12‐helices in α,γ‐hybrid peptides composed of achiral α‐aminoisobutyric acid (Aib) and 4‐aminoisocaproic acid (Aic, doubly homologated Aib) monomers in 1:1 alternation are reported. The 12‐helices were indicated by solution and crystal structural analyses of tetra‐ and heptapeptides. Surprisingly, single crystals of the longer nonapeptide displayed two different helix types: the novel...

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Foldamers to Nanotubes: Influence of Amino Acid Side Chains in the Hierarchical Assembly of α,γ⁴‐Hybrid Peptide Helices

Sandip V. Jadhav, Rajkumar Misra, Hosahudya N. Gopi

Chemistry – A European Journal > 20 > 50 > 16523 - 16528

Supramolecular assembly of various artificially folded 12‐helical architectures composed of γ⁴‐Val, γ⁴‐Leu and γ⁴‐Phe residues is investigated. In contrast to the 12‐helices composed of γ⁴‐Val and γ⁴‐Leu residues, the helices with γ⁴‐Phe residues displayed unique elongated nanotubular architectures. The elongated nanotube assembly was further explored as a template for biomineralization of silver...

article

Efficient Access to Enantiopure γ⁴‐Amino Acids with Proteinogenic Side‐Chains and Structural Investigation of γ⁴‐Asn and γ⁴‐Ser in Hybrid Peptide Helices

Sandip V. Jadhav, Rajkumar Misra, Sumeet K. Singh, Hosahudya N. Gopi

Chemistry – A European Journal > 19 > 48 > 16256 - 16262

Hybrid peptides composed of α‐ and β‐amino acids have recently emerged as new class of peptide foldamers. Comparatively, γ‐ and hybrid γ‐peptides composed of γ⁴‐amino acids are less studied than their β‐counterparts. However, recent investigations reveal that γ⁴‐amino acids have a higher propensity to fold into ordered helical structures. As amino acid side‐chain functional groups play a crucial role...

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Search results for: Rajkumar Misra

Exploring Helical Peptides and Foldamers for the Design of Metal Helix Frameworks: Current Trends and Future Perspectives

Exploring Helical Peptides and Foldamers for the Design of Metal Helix Frameworks: Current Trends and Future Perspectives

Exploiting Minimalistic Backbone Engineered γ‐Phenylalanine for the Formation of Supramolecular Co‐Polymer

From Folding to Assembly: Functional Supramolecular Architectures of Peptides Comprised of Non‐Canonical Amino Acids

From Folding to Assembly: Functional Supramolecular Architectures of Peptides Comprised of Non‐Canonical Amino Acids

Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers

Metal‐Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers

Metal‐Helix Frameworks from Short Hybrid Peptide Foldamers

Metal‐Helix Frameworks from Short Hybrid Peptide Foldamers

Artificial β‐Double Helices from Achiral γ‐Peptides

Artificial β‐Double Helices from Achiral γ‐Peptides

Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix

Structural Dimorphism of Achiral α,γ‐Hybrid Peptide Foldamers: Coexistence of 12‐ and 15/17‐Helices

Foldamers to Nanotubes: Influence of Amino Acid Side Chains in the Hierarchical Assembly of α,γ⁴‐Hybrid Peptide Helices

Efficient Access to Enantiopure γ⁴‐Amino Acids with Proteinogenic Side‐Chains and Structural Investigation of γ⁴‐Asn and γ⁴‐Ser in Hybrid Peptide Helices

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