Supramolecular Assemblies of Hydrogen‐Bonded Carboxylic Acid Dimers Mediated by Phenyl–Pentafluorophenyl Stacking Interactions

Gdaniec, Мaria; Jankowski, Wojciech; Milewska, Maria J.; Połoński, Tadeusz

doi:10.1002/anie.200351432

Cited by 111 publications

(85 citation statements)

References 44 publications

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“…Similar to the previously reported fluorinated benzoic acids which easily form either the homo-or hetero-dimers [24], two centrosymmetric single O-HÁ Á ÁO hydrogen bonds [HÁ Á ÁO1(Àx, Ày + 1, Àz + 2) 1.69(5), O2Á Á ÁO1(Àx, Ày + 1, Àz + 2) 2.716(3) Å , angle O-HÁ Á ÁO 174(4)8] combined into robust R 2 2 (8) synthon [25] govern the packing of the molecules into planar dimers. The dimers [28] to the plane of the above-mentioned hydrogen bonds, direct the herringbone assembling of the adjacent stacks (Fig.…”

Section: Resultssupporting

confidence: 75%

Chemoselectivity of cobalt-catalysed carbonylation—A reliable platform for the synthesis of fluorinated benzoic acids

Boyarskiy

Fonarı

Khaybulova

et al. 2010

Journal of Fluorine Chemistry

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Section: Resultssupporting

confidence: 75%

Chemoselectivity of cobalt-catalysed carbonylation—A reliable platform for the synthesis of fluorinated benzoic acids

Boyarskiy

Fonarı

Khaybulova

et al. 2010

Journal of Fluorine Chemistry

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“…For suitable hydrophobic interactions to facilitate self-assembly into supramolecular fibrils, we would add aromatic subunits onto the N and C termini. Phenyl and pentafluorophenyl groups emerged as good candidates because of strong noncovalent aromatic-stacking interactions between benzene and hexafluorobenzene (23,24). Thus, we decided to append L-pentaf luorophenylalanine (F 5 -Phe) and L-phenylalanine (F) onto the ends of 30-mer (GPO) 10 , as in 32-mer 1a (Fig.…”

Section: Resultsmentioning

confidence: 99%

Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions

Cejas

Kinney

Chen

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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128

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Collagens are integral structural proteins in animal tissues and play key functional roles in cellular modulation. We sought to discover collagen model peptides (CMPs) that would form triple helices and self-assemble into supramolecular fibrils exhibiting collagen-like biological activity without preorganizing the peptide chains by covalent linkages. This challenging objective was accomplished by placing aromatic groups on the ends of a representative 30-mer CMP, (GPO)10, as with L-phenylalanine and L-pentafluorophenylalanine in 32-mer 1a. Computational studies on homologous 29-mers 1a-d (one less GPO), as pairs of triple helices interacting head-to-tail, yielded stabilization energies in the order 1a > 1b > 1c > 1d, supporting the hypothesis that hydrophobic aromatic groups can drive CMP self-assembly. Peptides 1a-d were studied comparatively relative to structural properties and ability to stimulate human platelets. Although each 32-mer formed stable triple helices (CD) spectroscopy, only 1a and 1b self-assembled into micrometer-scale fibrils. Light microscopy images for 1a depicted long collagen-like fibrils, whereas images for 1d did not. Atomic force microscopy topographical images indicated that 1a and 1b self-organize into microfibrillar species, whereas 1c and 1d do not. Peptides 1a and 1b induced the aggregation of human blood platelets with a potency similar to type I collagen, whereas 1c was much less effective, and 1d was inactive (EC50 potency: 1a/1b Ͼ Ͼ 1c > 1d). Thus, 1a and 1b spontaneously self-assemble into thrombogenic collagen-mimetic materials because of hydrophobic aromatic interactions provided by the special end-groups. These findings have important implications for the design of biofunctional CMPs.biomaterial ͉ platelets ͉ structure-function ͉ supramolecular triplex T he self-association of peptides and proteins into well ordered supramolecular structures is of pivotal importance in normal physiology and pathophysiology, such as in the assembly of collagen fibrils (1), actin filaments (2), and amyloid fibrils (3, 4). Collagens, which constitute a ubiquitous protein family in animals, contribute an essential matrix component to soft tissues and bones (5, 6). A structural hallmark of many collagens is a rope-like triple helix, the architecture of which derives from the interplay of three proline-rich polypeptide strands (e.g., two ␣1 and one ␣2 for type I collagen) (6-8). In the core domain of the triple helix, the amino acid sequence G-X-Y is repeated multiple times, and each glycine amide NH forms a hydrogen bond with the X-position amide carbonyl on an adjacent strand. The X-and Y-positions are often populated by L-proline and 4(R)-hydroxy-L-proline (O; Hyp), respectively, with the latter stabilizing the triple helix by stereoelectronic effects (9) and water-bridged hydrogen bonds (10).To investigate collagen's structure and function, researchers have resorted to using synthetic collagen model peptides (CMPs)

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“…For dicarboxylic acids either 0D (cycles) or 1D (chains) structures can be created, while building blocks with more than two COOH groups could potentially be used to form any architectures. (8) dimers. This is one of the most stable associations observed for various carboxylic acids including cationic, anionic, radical and organometallic building blocks.…”

Section: Introductionmentioning

confidence: 98%

Mastering fundamentals of supramolecular design with carboxylic acids. Common lessons from X-ray crystallography and scanning tunneling microscopy

2011

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Hydrogen bonding is one of the most important non-covalent interactions in both biological (DNA, peptides, saccharides etc.) and artificial systems (various soft materials, host-guest architectures, molecular networks, etc.). Carboxylic acids are some of the most simple yet powerful hydrogen-bonding building blocks, that possess a particularly rich supramolecular chemistry. This tutorial review focuses on the structural diversity of supramolecular architectures accessible via hydrogen bonding of carboxylic acids, as observed both in single crystals using X-ray analysis and in monolayers on surfaces using scanning probe techniques. It provides a concise overview of the key concepts and principles of modern supramolecular design and is given in the form of case studies of finely selected literature examples, covering formation of macrocycles, chains, ladders, rotaxanes, catenanes, various 2D and 3D nets, host-guest systems and some applications thereof.

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Supramolecular Assemblies of Hydrogen‐Bonded Carboxylic Acid Dimers Mediated by Phenyl–Pentafluorophenyl Stacking Interactions

Cited by 111 publications

References 44 publications

Chemoselectivity of cobalt-catalysed carbonylation—A reliable platform for the synthesis of fluorinated benzoic acids

Chemoselectivity of cobalt-catalysed carbonylation—A reliable platform for the synthesis of fluorinated benzoic acids

Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions

Mastering fundamentals of supramolecular design with carboxylic acids. Common lessons from X-ray crystallography and scanning tunneling microscopy

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