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Keiichi Noguchi

Publications and source records attributed to Keiichi Noguchi.

17 recordsLinked to original sources
PubMed2006

Enantioselective Synthesis of Tetra-ortho-Substituted Axially Chiral Biaryls through Rhodium-Catalyzed Double [2 + 2 + 2] Cycloaddition.

[reaction: see text] We have established an enantioselective synthesis of both C2 symmetric and unsymmetric tetra-ortho-substituted axially chiral biaryls through rhodium-catalyzed double [2 + 2 + 2] cycloaddition (up to >99% ee). This method serves as an attractive new route to enantioenriched tetra-ortho-substituted axially chiral biaryls in view of the one-step access to substrate diynes and tetraynes starting from readily available alkynes.

Journal Article↗
PubMed2006

Enantioselective synthesis of axially chiral anilides through rhodium-catalyzed [2+2+2] cycloaddition of 1,6-diynes with trimethylsilylynamides.

We have developed a rhodium-catalyzed enantioselective intermolecular [2+2+2] cycloaddition of 1,6-diynes with trimethylsilylynamides for the synthesis of axially chiral anilides. The axial chirality is constructed at the formation of benzene rings with high enantioselectivity (up to 98% ee). It should be noted that the present reaction employs the readily prepared trimethylsilylynamides starting from commercially available bis(trimethysilyl)acetylene and the trimethylsilyl group of the product anilides is expected to be utilized for further functionalization.

Journal Article↗
PubMed2006

Revision of collagen molecular structure.

Based on the fiber diffraction data from native collagen, Rich and Crick proposed the 10/3-helical model with a 28.6 A axial repeat in 1955 (Rich A.; Crick, F. H. C. Nature (Lond) 1955, 176, 915-916). We obtained the 7/2-helical structure with a 20 A axial repeat from the single crystal analysis of (Pro-Pro-Gly)(10). Since the latter structure could explain fiber diffraction patterns from native collagen, we proposed this structure as a new model for collagen in 1977 (Okuyama et al., Polym J 1977, 9, 341-343). These two structural models were refined against observed continuous intensity data from native collagen using a linked-atom least-squares method. It was found that the diffraction data from native collagen could be explained by the 7/2-helical model better than, or at least the same as, the prevailing 10/3-helical model. Together with the evidence that recent single crystal analyses of many model peptides have supported the 7/2-helical model and there was no such active support for the 10/3-helical model, it was concluded that the average molecular structure of native collagen seems to be closer to the 7/2-helical symmetry than the other one.

Animals↗
PubMed2006

Helical twists of collagen model peptides.

Average helical twists were calculated by the method of Sugeta and Miyazawa (Biopolymers 1967, 5, 673-679) for all of the collagen model peptides analyzed to date. Calculation of the helical twists of all triplets in each peptide strand provided novel insights for several model peptides. In the (Pro-Pro-Gly)n (n = 9 and 10), the helical twists showed cyclic fluctuations between 40 and 65 degrees with a 20 A period, suggesting that their molecular conformations were close enough to the ideal 7/2-helix to show the helical repeat of 20 A. Rather small helical twists in the guest regions of IBP in complex and T3-785 were attributed to the interaction with Integrin I domain and a relaxed conformation caused by three consecutive triplets lacking imino acid residues, respectively. Although most of the triplets used in this study were imino acid-rich triplets, helical twists were scattered in a wide range from 30 to 70 degrees with an overall average of 52.6 degrees . This distribution of helical twists indicated a strong preference for the 7/2-helical conformation (51.4 degrees ) rather than the 10/3-helical model (36 degrees ).

Collagen↗
PubMed2005

Rhodium-catalyzed chemo-, regio-, and enantioselective [2 + 2 + 2] cycloaddition of alkynes with isocyanates.

[reaction: see text] We have developed a cationic rhodium(I)/modified-BINAP complex-catalyzed chemoselective [2 + 2 + 2] cycloaddition of alkynes with isocyanates leading to a wide range of 2-pyridones. This method was successfully applied to the chemo-, regio-, and enantioselective synthesis of axially chiral 2-pyridones from unsymmetrical alpha,omega-diynes, bearing an ortho-substituted phenyl at one terminal position, and alkyl isocyanates.

Journal Article↗
PubMed2005

Enantioselective synthesis of axially chiral biaryls through rhodium-catalyzed complete intermolecular cross-cyclotrimerization of internal alkynes.

[reaction: see text] We have developed a cationic rhodium(I)/H8-BINAP complex-catalyzed complete intermolecular cross-cyclotrimerization of internal alkynes with dialkyl acetylenedicarboxylates. This reaction was successfully applied to enantioselective synthesis of axially chiral biaryls utilizing internal alkynes bearing ortho-substituted phenyl and acetoxymethyl in each terminal position. The axial chirality is constructed at the formation of benzene rings with high enantioselectivity (up to 96% ee).

Journal Article↗
PubMed2005

Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3.

The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.

Collagen↗
PubMed2004

Molecular and crystal structures of chitosan/HI type I salt determined by X-ray fiber diffraction.

The three-dimensional structure of chitosan/HI type I salt was determined by the X-ray fiber diffraction technique and linked-atom least-squares refinement method. Two polymer chains and four iodide ions (I(-)) crystallized in a monoclinic unit cell with dimensions a = 9.46(2), b = 9.79(2)], c (fiber axis)=10.33(2)A, beta = 105.2(2) degrees and a space group P2(1). Chitosan chains adopted an extended twofold helical conformation that was stabilized by O-3...O-5 hydrogen bonds, and the O-6 atom adopted nearly gt orientation. Polymer chains zigzag along the b-axis and directly connect to each other by N-2...O-6 hydrogen bonds. Two columns of iodide ions were shown to pack at the bending points of the zigzag sheets, and their locations are closely related to those of water columns in the hydrated chitosan. The iodide ions stabilized the salt structure by forming hydrogen bonds with the N-2 and O-6 atoms of the polymer chains together with an electrostatic interaction between N-2 and the iodide ions.

Animals↗
PubMed2004

Plausible molecular and crystal structures of chitosan/HI type II salt.

Chitosan/HI type II salt prepared from crab tendon was investigated by X-ray fiber diffraction. Two polymer chains and 16 iodide ions (I(-)) crystallized in a tetragonal unit cell with lattice parameters of a = b = 10.68(3), c (fiber axis) = 40.77(13) A, and a space group P4(1). Chitosan forms a fourfold helix with a 40.77 A fiber period having a disaccharide as the helical asymmetric unit. One of the O-3... O-5 intramolecular hydrogen bonds at the glycosidic linkage is weakened by interacting with iodide ions, which seems to cause the polymer to take the 4/1-helical symmetry rather than the extended 2/1-helix. The plausible orientations of two O-6 atoms in the helical asymmetric unit were found to be gt and gg. Two chains are running through at the corner and the center of the unit cell along the c-axis. They are linked by hydrogen bonds between N-21 and O-61 atoms. Two out of four independent iodide ions are packed between the corner chains while the other two are packed between the corner and center chains when viewing through the ab-plane. The crystal structure of the salt is stabilized by hydrogen bonds between these iodide ions and N-21, N-22, O-32, O-61, O-62 of the polymer chains.

Animals↗
PubMed2004

Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 A resolution: implications for proline ring puckering.

Triple-helical structures of (Pro-Hyp-Gly)n (n = 10, 11) at 100 K and room temperature (RT) were analyzed at 1.26 A resolution by using synchrotron radiation data. Totals of 49 and 42 water molecules per seven triplets in an asymmetric unit were found for the structures at 100 K and RT, respectively. These water molecules were classified into two groups, those in the first and second hydration shells. Although there was no significant difference between water molecules in the first shell at 100 K and those at RT, a significant difference between those in the second shell was observed. That is, the number of water molecules at RT decreased to one half and the average distance from peptide chains at RT became longer by about 0.3 A. On the other hand, of seven triplets in an asymmetric unit, three proline residues at the X position at 100 K clearly showed an up-puckering conformation, as opposed to the recent propensity-based hypothesis for the stabilization and destabilization of triple-helical structures by proline hydroxylation. This puckering was attributed to the interaction between proline rings and the surrounding water molecules at 100 K, which is much weaker at RT, as shown by longer average distance from peptide chains.

Collagen↗
PubMed2003

Two different molecular conformations found in chitosan type II salts.

The type II structure of chitosan acidic salts prepared from crab tendon in solid state was studied using an X-ray fiber diffraction technique together with the linked-atom least-squares (LALS) technique. The cylindrical Patterson method was applied to confirm the molecular conformation of the chitosan. It was shown that there are two different helical conformations for type II salts. One is the relaxed twofold helix having a tetrasaccharide as an asymmetric unit as found in chitosan.HCl salt, which was previously reported as a conformation of chitosan.HCOOH salt. The other is the fourfold helix having a disaccharide as an asymmetric unit newly found in chitosan.HI salt.

Carbohydrate Conformation↗
PubMed2003

WinLALS for a linked-atom least-square refinement program for helical polymers on WINDOWS PCs.

Fiber diffraction dada from polymers are sufficiently different in kind and quantity from single crystal data as to warrant analyses with a different emphasis: refinement of competing molecular models where torsion angles and bond angles are the explicit variables rather than atomic coordinates. The first linked-atom least-squares (LALS) refinement program had been devolved at Arnott's laboratories at King's College London [Arnott, S., Wonacott, A.J., 1966a. Polymer 7, 157] on mainframe and several revised versions were maintained at Purdue University [Smith, P.J.C., Arnott, S., 1978. Acta Crystallogr. Sect. A 34, 3; Chandrasekan, R. 2000. LALS Users Manual, Whistler Centre for Carbohydrate Researchm Purdue University, West Lafayette, IN] on workstation. Today the LALS users have to choose correctly any one program that they want to use, trigonometric or Bessel functions, from some versions. To develop a new WinLALS program based on the dimensioned version of the latest LALS2000 program [LALS Users Manual (2000)], we reviewed all the mathematical expressions and corrected the optimization of the non-bonded atomic contact terms. The WinLALS is coded with FORTRAN 90 and runs on MICROSOFT-WINDOWS PCs and the many amendments including changing input/output assignments, expanding array sizes, arranging that the update files have all output parameters of each cycle, and correcting several bugs are performed. This paper describes the mathematical expressions in detail employed in WinLALS and compares results of its applications obtained with those obtained earlier.

Journal Article↗