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Covalent Self-Assembly and One-Step Photocrosslinking of Tyrosine-Rich Oligopeptides to Form Diverse Nanostructures.

Angewandte Chemie (International ed. in English)

Min KI, Yun G, Jang Y, Kim KR, Ko YH, Jang HS, Lee YS, Kim K, Kim DP.
PMID: 27062089
Angew Chem Int Ed Engl. 2016 Jun 06;55(24):6925-8. doi: 10.1002/anie.201601675. Epub 2016 Apr 08.

We present covalently self-assembled peptide hollow nanocapsule and peptide lamella. These biomimetic dityrosine peptide nanostructures are synthesized by one-step photopolymerization of a tyrosine-rich short peptide without the aid of a template. This simple approach offers direct synthesis of fluorescent...

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Min KI, Yun G, Jang Y, et al. Covalent Self-Assembly and One-Step Photocrosslinking of Tyrosine-Rich Oligopeptides to Form Diverse Nanostructures. Angew Chem Int Ed Engl. 2016;55(24):6925-8doi: 10.1002/anie.201601675.
Min, K. I., Yun, G., Jang, Y., Kim, K. R., Ko, Y. H., Jang, H. S., Lee, Y. S., Kim, K., & Kim, D. P. (2016). Covalent Self-Assembly and One-Step Photocrosslinking of Tyrosine-Rich Oligopeptides to Form Diverse Nanostructures. Angewandte Chemie (International ed. in English), 55(24), 6925-8. https://doi.org/10.1002/anie.201601675
Min, Kyoung-Ik, et al. "Covalent Self-Assembly and One-Step Photocrosslinking of Tyrosine-Rich Oligopeptides to Form Diverse Nanostructures." Angewandte Chemie (International ed. in English) vol. 55,24 (2016): 6925-8. doi: https://doi.org/10.1002/anie.201601675
Min KI, Yun G, Jang Y, Kim KR, Ko YH, Jang HS, Lee YS, Kim K, Kim DP. Covalent Self-Assembly and One-Step Photocrosslinking of Tyrosine-Rich Oligopeptides to Form Diverse Nanostructures. Angew Chem Int Ed Engl. 2016 Jun 06;55(24):6925-8. doi: 10.1002/anie.201601675. Epub 2016 Apr 08. PMID: 27062089.
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Isolation and biochemical characterization of bradykinin-potentiating peptides from .

The journal of venomous animals and toxins including tropical diseases

Fucase TM, Sciani JM, Cavalcante I, Viala VL, Chagas BB, Pimenta DC, Spencer PJ.
PMID: 28670326
J Venom Anim Toxins Incl Trop Dis. 2017 Jun 26;23:33. doi: 10.1186/s40409-017-0124-9. eCollection 2017.

BACKGROUND: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs...

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Fucase TM, Sciani JM, Cavalcante I, et al. Isolation and biochemical characterization of bradykinin-potentiating peptides from . J Venom Anim Toxins Incl Trop Dis. 2017;23:33doi: 10.1186/s40409-017-0124-9.
Fucase, T. M., Sciani, J. M., Cavalcante, I., Viala, V. L., Chagas, B. B., Pimenta, D. C., & Spencer, P. J. (2017). Isolation and biochemical characterization of bradykinin-potentiating peptides from . The journal of venomous animals and toxins including tropical diseases, 2333. https://doi.org/10.1186/s40409-017-0124-9
Fucase, Tamara M, et al. "Isolation and biochemical characterization of bradykinin-potentiating peptides from ." The journal of venomous animals and toxins including tropical diseases vol. 23 (2017): 33. doi: https://doi.org/10.1186/s40409-017-0124-9
Fucase TM, Sciani JM, Cavalcante I, Viala VL, Chagas BB, Pimenta DC, Spencer PJ. Isolation and biochemical characterization of bradykinin-potentiating peptides from . J Venom Anim Toxins Incl Trop Dis. 2017 Jun 26;23:33. doi: 10.1186/s40409-017-0124-9. eCollection 2017. PMID: 28670326; PMCID: PMC5485657.
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ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins.

Journal of chemical theory and computation

Cerutti DS, Swope WC, Rice JE, Case DA.
PMID: 25328495
J Chem Theory Comput. 2014 Oct 14;10(10):4515-4534. doi: 10.1021/ct500643c. Epub 2014 Sep 18.

We present the ff14ipq force field, implementing the previously published IPolQ charge set for simulations of complete proteins. Minor modifications to the charge derivation scheme and van der Waals interactions between polar atoms are introduced. Torsion parameters are developed...

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Cerutti DS, Swope WC, Rice JE, et al. ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins. J Chem Theory Comput. 2014;10(10):4515-4534doi: 10.1021/ct500643c.
Cerutti, D. S., Swope, W. C., Rice, J. E., & Case, D. A. (2014). ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins. Journal of chemical theory and computation, 10(10), 4515-4534. https://doi.org/10.1021/ct500643c
Cerutti, David S, et al. "ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins." Journal of chemical theory and computation vol. 10,10 (2014): 4515-4534. doi: https://doi.org/10.1021/ct500643c
Cerutti DS, Swope WC, Rice JE, Case DA. ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins. J Chem Theory Comput. 2014 Oct 14;10(10):4515-4534. doi: 10.1021/ct500643c. Epub 2014 Sep 18. PMID: 25328495; PMCID: PMC4196740.
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Enhanced Conformational Sampling in Molecular Dynamics Simulations of Solvated Peptides: Fragment-Based Local Elevation Umbrella Sampling.

Journal of chemical theory and computation

Hansen HS, Daura X, Hünenberger PH.
PMID: 26616064
J Chem Theory Comput. 2010 Sep 14;6(9):2598-621. doi: 10.1021/ct1003059.

A new method, fragment-based local elevation umbrella sampling (FB-LEUS), is proposed to enhance the conformational sampling in explicit-solvent molecular dynamics (MD) simulations of solvated polymers. The method is derived from the local elevation umbrella sampling (LEUS) method [ Hansen...

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Hansen HS, Daura X, Hünenberger PH. Enhanced Conformational Sampling in Molecular Dynamics Simulations of Solvated Peptides: Fragment-Based Local Elevation Umbrella Sampling. J Chem Theory Comput. 2010;6(9):2598-621doi: 10.1021/ct1003059.
Hansen, H. S., Daura, X., & Hünenberger, P. H. (2010). Enhanced Conformational Sampling in Molecular Dynamics Simulations of Solvated Peptides: Fragment-Based Local Elevation Umbrella Sampling. Journal of chemical theory and computation, 6(9), 2598-621. https://doi.org/10.1021/ct1003059
Hansen, Halvor S, et al. "Enhanced Conformational Sampling in Molecular Dynamics Simulations of Solvated Peptides: Fragment-Based Local Elevation Umbrella Sampling." Journal of chemical theory and computation vol. 6,9 (2010): 2598-621. doi: https://doi.org/10.1021/ct1003059
Hansen HS, Daura X, Hünenberger PH. Enhanced Conformational Sampling in Molecular Dynamics Simulations of Solvated Peptides: Fragment-Based Local Elevation Umbrella Sampling. J Chem Theory Comput. 2010 Sep 14;6(9):2598-621. doi: 10.1021/ct1003059. PMID: 26616064.
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Bone site-specific delivery of siRNA.

Journal of biomedical research

Liu X.
PMID: 26642236
J Biomed Res. 2016 Jul;30(4):264-71. doi: 10.7555/JBR.30.20150110. Epub 2015 Nov 18.

Small interfering RNAs (siRNA) have enormous potential as therapeutics to target and treat various bone disorders such as osteoporosis and cancer bone metastases. However, effective and specific delivery of siRNA therapeutics to bone and bone-specific cells in vivo is...

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Liu X. Bone site-specific delivery of siRNA. J Biomed Res. 2015;30(4):264-71doi: 10.7555/JBR.30.20150110.
Liu, X. (2016). Bone site-specific delivery of siRNA. Journal of biomedical research, 30(4), 264-71. https://doi.org/10.7555/JBR.30.20150110
Liu, Xinli. "Bone site-specific delivery of siRNA." Journal of biomedical research vol. 30,4 (2016): 264-71. doi: https://doi.org/10.7555/JBR.30.20150110
Liu X. Bone site-specific delivery of siRNA. J Biomed Res. 2016 Jul;30(4):264-71. doi: 10.7555/JBR.30.20150110. Epub 2015 Nov 18. PMID: 26642236; PMCID: PMC4946317.
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Charge Tunneling along Short Oligoglycine Chains.

Angewandte Chemie (International ed. in English)

Baghbanzadeh M, Bowers CM, Rappoport D, Żaba T, Gonidec M, Al-Sayah MH, Cyganik P, Aspuru-Guzik A, Whitesides GM.
PMID: 26450132
Angew Chem Int Ed Engl. 2015 Dec 01;54(49):14743-7. doi: 10.1002/anie.201507271. Epub 2015 Oct 09.

This work examines charge transport (CT) through self-assembled monolayers (SAMs) of oligoglycines having an N-terminal cysteine group that anchors the molecule to a gold substrate, and demonstrate that CT is rapid (relative to SAMs of n-alkanethiolates). Comparisons of rates...

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Baghbanzadeh M, Bowers CM, Rappoport D, et al. Charge Tunneling along Short Oligoglycine Chains. Angew Chem Int Ed Engl. 2015;54(49):14743-7doi: 10.1002/anie.201507271.
Baghbanzadeh, M., Bowers, C. M., Rappoport, D., Żaba, T., Gonidec, M., Al-Sayah, M. H., Cyganik, P., Aspuru-Guzik, A., & Whitesides, G. M. (2015). Charge Tunneling along Short Oligoglycine Chains. Angewandte Chemie (International ed. in English), 54(49), 14743-7. https://doi.org/10.1002/anie.201507271
Baghbanzadeh, Mostafa, et al. "Charge Tunneling along Short Oligoglycine Chains." Angewandte Chemie (International ed. in English) vol. 54,49 (2015): 14743-7. doi: https://doi.org/10.1002/anie.201507271
Baghbanzadeh M, Bowers CM, Rappoport D, Żaba T, Gonidec M, Al-Sayah MH, Cyganik P, Aspuru-Guzik A, Whitesides GM. Charge Tunneling along Short Oligoglycine Chains. Angew Chem Int Ed Engl. 2015 Dec 01;54(49):14743-7. doi: 10.1002/anie.201507271. Epub 2015 Oct 09. PMID: 26450132.
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Hypotensive and vasorelaxant effects of sericin-derived oligopeptides in rats.

ISRN pharmacology

Onsa-Ard A, Shimbhu D, Tocharus J, Sutheerawattananonda M, Pantan R, Tocharus C.
PMID: 24312733
ISRN Pharmacol. 2013 Nov 07;2013:717529. doi: 10.1155/2013/717529. eCollection 2013.

Sericin-derived oligopeptides obtained from silk cocoons were investigated for the in vivo hypotensive effect and investigated for the underlying mechanism involved in vasodilation in isolated rat thoracic aorta. In normotensive anesthetized rats, oligopeptides induced an immediate and transient hypotensive...

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Onsa-Ard A, Shimbhu D, Tocharus J, et al. Hypotensive and vasorelaxant effects of sericin-derived oligopeptides in rats. ISRN Pharmacol. 2013;2013:717529doi: 10.1155/2013/717529.
Onsa-Ard, A., Shimbhu, D., Tocharus, J., Sutheerawattananonda, M., Pantan, R., & Tocharus, C. (2013). Hypotensive and vasorelaxant effects of sericin-derived oligopeptides in rats. ISRN pharmacology, 2013717529. https://doi.org/10.1155/2013/717529
Onsa-Ard, Amnart, et al. "Hypotensive and vasorelaxant effects of sericin-derived oligopeptides in rats." ISRN pharmacology vol. 2013 (2013): 717529. doi: https://doi.org/10.1155/2013/717529
Onsa-Ard A, Shimbhu D, Tocharus J, Sutheerawattananonda M, Pantan R, Tocharus C. Hypotensive and vasorelaxant effects of sericin-derived oligopeptides in rats. ISRN Pharmacol. 2013 Nov 07;2013:717529. doi: 10.1155/2013/717529. eCollection 2013. PMID: 24312733; PMCID: PMC3839117.
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Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides.

Planta

Higgins CF, Payne JW.
PMID: 24414048
Planta. 1978 Jan;138(3):211-5. doi: 10.1007/BF00386813.

The uptake of a variety of physiological di- and oligopeptides by germinating barley (Hordeum vulgare L.) embryos is described. Peptides as large as pentaalanine can be absorbed. Evidence is presented suggesting the peptides are absorbed intact and subsequently undergo...

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Higgins CF, Payne JW. Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides. Planta. 1978;138(3):211-5doi: 10.1007/BF00386813.
Higgins, C. F., & Payne, J. W. (1978). Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides. Planta, 138(3), 211-5. https://doi.org/10.1007/BF00386813
Higgins, C F, and Payne, J W. "Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides." Planta vol. 138,3 (1978): 211-5. doi: https://doi.org/10.1007/BF00386813
Higgins CF, Payne JW. Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides. Planta. 1978 Jan;138(3):211-5. doi: 10.1007/BF00386813. PMID: 24414048.
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Optical rotatory dispersion properties of nucleic acid complexes with the oligopeptide antibiotics distamycin A and netropsin.

FEBS letters

Zimmer C, Luck G.
PMID: 11945427
FEBS Lett. 1970 Oct;10(5):339-342. doi: 10.1016/0014-5793(70)80467-7.

ORD measurements of nucleic acids in the presence of the oligopeptides netropsin and distamycin A have indicated association of the antibiotics with DNA and strong conformational changes of the DNA structure with specificity to AT-rich helical regions. The RNA...

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Zimmer C, Luck G. Optical rotatory dispersion properties of nucleic acid complexes with the oligopeptide antibiotics distamycin A and netropsin. FEBS Lett. 1970;10(5):339-342doi: 10.1016/0014-5793(70)80467-7.
Zimmer, C., & Luck, G. (1970). Optical rotatory dispersion properties of nucleic acid complexes with the oligopeptide antibiotics distamycin A and netropsin. FEBS letters, 10(5), 339-342. https://doi.org/10.1016/0014-5793(70)80467-7
Zimmer, C, and Luck, G. "Optical rotatory dispersion properties of nucleic acid complexes with the oligopeptide antibiotics distamycin A and netropsin." FEBS letters vol. 10,5 (1970): 339-342. doi: https://doi.org/10.1016/0014-5793(70)80467-7
Zimmer C, Luck G. Optical rotatory dispersion properties of nucleic acid complexes with the oligopeptide antibiotics distamycin A and netropsin. FEBS Lett. 1970 Oct;10(5):339-342. doi: 10.1016/0014-5793(70)80467-7. PMID: 11945427.
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Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation.

Proceedings of the National Academy of Sciences of the United States of America

Mustardy L, Los DA, Gombos Z, Murata N.
PMID: 11607709
Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10524-7. doi: 10.1073/pnas.93.19.10524.

There are four acyl-lipid desaturases in the cyanobacterium Synechocystis sp. PCC 6803. Each of these desaturases introduces a double bond at a specific position, such as the Delta6, Delta9, Delta12, or omicron3 position, in C18 fatty acids. The localization...

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Mustardy L, Los DA, Gombos Z, et al. Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation. Proc Natl Acad Sci U S A. 1996;93(19):10524-7doi: 10.1073/pnas.93.19.10524.
Mustardy, L., Los, D. A., Gombos, Z., & Murata, N. (1996). Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation. Proceedings of the National Academy of Sciences of the United States of America, 93(19), 10524-7. https://doi.org/10.1073/pnas.93.19.10524
Mustardy, L, et al. "Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation." Proceedings of the National Academy of Sciences of the United States of America vol. 93,19 (1996): 10524-7. doi: https://doi.org/10.1073/pnas.93.19.10524
Mustardy L, Los DA, Gombos Z, Murata N. Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10524-7. doi: 10.1073/pnas.93.19.10524. PMID: 11607709; PMCID: PMC38419.
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Molecular cloning and antiserum development of cyclin box in the brown tide alga Aureococcus anophagefferens.

Marine biotechnology (New York, N.Y.)

Lin S, Magaletti E, Carpenter EJ.
PMID: 14961181
Mar Biotechnol (NY). 2000 Nov;2(6):577-86. doi: 10.1007/s101260000044.

Cyclins can be useful cell cycle markers for growth rate studies on harmful algal blooms. In this study, a gene fragment corresponding to cyclin box was cloned for the brown tide alga Aureococcus anophagefferens. This algal gene fragment, designated...

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Lin S, Magaletti E, Carpenter EJ. Molecular cloning and antiserum development of cyclin box in the brown tide alga Aureococcus anophagefferens. Mar Biotechnol (NY). 2000;2(6):577-86doi: 10.1007/s101260000044.
Lin, S., Magaletti, E., & Carpenter, E. J. (2000). Molecular cloning and antiserum development of cyclin box in the brown tide alga Aureococcus anophagefferens. Marine biotechnology (New York, N.Y.), 2(6), 577-86. https://doi.org/10.1007/s101260000044
Lin, S, et al. "Molecular cloning and antiserum development of cyclin box in the brown tide alga Aureococcus anophagefferens." Marine biotechnology (New York, N.Y.) vol. 2,6 (2000): 577-86. doi: https://doi.org/10.1007/s101260000044
Lin S, Magaletti E, Carpenter EJ. Molecular cloning and antiserum development of cyclin box in the brown tide alga Aureococcus anophagefferens. Mar Biotechnol (NY). 2000 Nov;2(6):577-86. doi: 10.1007/s101260000044. PMID: 14961181.
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Portage of various compounds into bacteria by attachment to glycine residues in peptides.

Proceedings of the National Academy of Sciences of the United States of America

Kingsbury WD, Boehm JC, Perry D, Gilvarg C.
PMID: 16593491
Proc Natl Acad Sci U S A. 1984 Jul;81(14):4573-6. doi: 10.1073/pnas.81.14.4573.

Synthetic di- and oligopeptides are described that contain nucleophilic moieties attached to the alpha carbon of a glycine residue. These peptides are accepted by the peptide transport systems of Escherichia coli (and other microorganisms) and are capable of being...

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Kingsbury WD, Boehm JC, Perry D, et al. Portage of various compounds into bacteria by attachment to glycine residues in peptides. Proc Natl Acad Sci U S A. 1984;81(14):4573-6doi: 10.1073/pnas.81.14.4573.
Kingsbury, W. D., Boehm, J. C., Perry, D., & Gilvarg, C. (1984). Portage of various compounds into bacteria by attachment to glycine residues in peptides. Proceedings of the National Academy of Sciences of the United States of America, 81(14), 4573-6. https://doi.org/10.1073/pnas.81.14.4573
Kingsbury, W D, et al. "Portage of various compounds into bacteria by attachment to glycine residues in peptides." Proceedings of the National Academy of Sciences of the United States of America vol. 81,14 (1984): 4573-6. doi: https://doi.org/10.1073/pnas.81.14.4573
Kingsbury WD, Boehm JC, Perry D, Gilvarg C. Portage of various compounds into bacteria by attachment to glycine residues in peptides. Proc Natl Acad Sci U S A. 1984 Jul;81(14):4573-6. doi: 10.1073/pnas.81.14.4573. PMID: 16593491; PMCID: PMC345633.
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Showing 1 to 12 of 269 entries