Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Peptide Bonds02:43

Peptide Bonds

84.0K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
84.0K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.7K
Alkyl Halides02:45

Alkyl Halides

20.4K
Structural Properties
Alkyl halides are halogen-substituted alkanes wherein one or more hydrogen atoms of an alkane is replaced by a halogen atom such as fluorine, chlorine, bromine, or iodine. The carbon atom in an alkyl halide is bonded to the halogen atom, which is sp3-hybridized and exhibits a tetrahedral shape.
Unlike alkyl halides, compounds in which a halogen atom is bonded to an sp2 -hybridized carbon atom of a carbon-carbon double bond (C=C) are called vinyl halides. Whereas aryl...
20.4K
Protein Folding01:25

Protein Folding

11.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.7K

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Surface-Induced Donor-Acceptor Charge-Transfer Interaction in Crystallization-Driven Two-Dimensional Assembly of Poly(L-Lactide) and Its Impact on Piezoelectric Performance.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Circularly Polarized Luminescence (CPL)-Active Homo- and Heterostructures by Surface-Catalyzed Secondary Supramolecular Polymerization.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Photosensitizer-pendant biotinylated polyester as a nanocarrier for targeted photodynamic therapy.

Journal of materials chemistry. B·2025
Same author

Crystallization-driven two-dimensional assemblies from a phenothiazine-conjugated poly(l-lactide): redox-responsive tunable emission, white-light harvesting and surface-enabled nanoparticle decoration.

Chemical science·2025
Same author

Correction to "Crafting Precision: Design and Fabrication of Xurography-Driven Microfluidic Platform for Exploring Neuron Culture and Targeted Drug Screening".

ACS chemical neuroscience·2025
Same author

Crafting Precision: Design and Fabrication of a Xurography-Driven Microfluidic Platform for Exploring Neuron Culture and Targeted Drug Screening.

ACS chemical neuroscience·2025

関連する実験動画

Updated: Feb 20, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.5K

調節ペプチドは,ハロゲン結合およびその他のハロゲン効果によって自己組み立てを行う.

Anindyasundar Adak1,2, Payel Khanra1, Anindita Das1

  • 1School of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation of Science (IACS), Jadavpur, Kolkata, INDIA.

Chemistry (Weinheim an der Bergstrasse, Germany)
|February 19, 2026
PubMed
まとめ

この研究は,ハロゲン結合やその他のハロゲン効果がペプチドの自己組み立てにどのように影響するかを示しています. ヨウ素を含むペプチドは,フッ素類のペプチドと比較して,より高い安定性と明確な自己組み立てメカニズムを示しています.

キーワード:
ハロゲン結合によるハロゲン結合です.水素結合による水素結合です.ナノファイバーナノファイバーペプチドアセンブリのペプチドアセンブリについて超分子ゲルである.

さらに関連する動画

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
05:24

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

1.7K
Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

7.8K

関連する実験動画

Last Updated: Feb 20, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.5K
Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
05:24

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

1.7K
Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

7.8K

科学分野:

  • バイオマテリアル科学 バイオマテリアル科学
  • 超分子化学 超分子化学
  • 化学生物学 化学生物学とは

背景:

  • ペプチドの自己組み立ては,高度な生体材料の開発に不可欠です.
  • 水素結合 (HB) やハロゲン結合 (XB) などの非共性相互作用を理解することは,自己組み立てを制御する鍵です.
  • 直接的なXBを超えたハロゲン効果は,分子行動に大きな影響を与えることができます.

研究 の 目的:

  • ハロゲン結合 (XB) およびその他のハロゲン効果によるペプチド自己組成の調節を調査する.
  • 機能化されたペプチドにおけるヨウ素とフッ素の自己組立特性に対する影響を比較する.
  • ペプチドの自己組織化におけるXB,HB,および水害性相互作用の相互作用を解明する.

主な方法:

  • 共通のFFKモチーフを持つ3つの機能化されたペンタペプチドの合成.
  • テトラフルオロイオドフェニル (TFIP) 分子がXBドナーとして組み込まれる.
  • 総合的な研究を使用して,自己組み立て,熱安定性,粘弾性特性の特徴付け.

主要な成果:

  • ヒスティジンで機能化されたペプチドは有意なC-I··NXBを示したが,フェニララニンで終了したペプチドは無視できるXBを示した.
  • ヨウ素を含むペプチドは,フッ素類のペプチドよりも高い安定性と強固な粘弾性特性を示した.
  • 異なる自己組み立てメカニズム (協同型対同型) が観察され,これはヨウ素の性および極化性によるものである.

結論:

  • ハロゲン結合やその他のハロゲン効果は,水素結合と連携して,ペプチドの自己組み立てを調節することができます.
  • ヨウ素のユニークな特性により,安定性が向上し,フッ素と比較して異なる自己組み立て行動がもたらされます.
  • XB,HB,および水害性相互作用の微妙なバランスがペプチドの自己組織を微調整します.