Skip to main content Accessibility help

We use cookies to distinguish you from other users and to provide you with a better experience on our websites. Close this message to accept cookies or find out how to manage your cookie settings.

Close cookie message
×
Hostname: page-component-cd9895bd7-jn8rn Total loading time: 0 Render date: 2025-01-03T19:03:17.406Z Has data issue: false hasContentIssue false

20 - Plausible lipid-like peptides: prebiotic molecular self-assembly in water

Published online by Cambridge University Press:  18 December 2009

By
Shuguang Zhang
Edited by
John D. Barrow ,
Simon Conway Morris ,
Stephen J. Freeland  and
Charles L. Harper, Jr
Shuguang Zhang
Affiliation:
Center for Biomedical Engineering and the Center for Bits and Atoms, Massachusetts Institute of Technology
John D. Barrow
Affiliation:
University of Cambridge
Simon Conway Morris
Affiliation:
University of Cambridge
Stephen J. Freeland
Affiliation:
University of Maryland, Baltimore
Charles L. Harper, Jr
Affiliation:
John Templeton Foundation
Get access

Summary

Introduction

Life as we know it today completely depends on water. Without water, life would be either impossible or totally different. Thus, a deep understanding of the relationship between water and other simple building blocks of life is crucial to gain insight into how prebiotic life forms could have originated and evolved and whether the physical laws of this universe are in any way predisposed to the emergence of life (Henderson, 1913, 1917; Eisenberg and Kauzmann, 1985; Ball, 2001).

It is unlikely that under prebiotic conditions the complex and sophisticated biomacromolecules commonplace in modern biochemistry would have existed. Thus, research into the origin of life is intimately associated with the search for plausible systems that are much simpler than those we see today. However, it is also plausible that these simple building blocks of life might have been amphiphilic molecules in which water could have had an enormous influence on their prebiotic molecular selection and evolution, because water can either form clathrate structures or drive these simplest molecules together (Ball, 2001).

Structure of water

Water is both simple and complex. It is simple because it consists of only one oxygen atom and two hydrogen atoms (see Figure 20.1). But at the same time it exhibits highly complex molecular behavior (far exceeding the multibody problem in mathematics, planetary science, and astrophysics) wherever numerous water molecules interact dynamically (Eisenberg and Kauzmann, 1985; Ball, 2001).

Type
Chapter
Information
Fitness of the Cosmos for Life
Biochemistry and Fine-Tuning
 , pp. 440 - 455
Publisher: Cambridge University Press
Print publication year: 2007

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Anders, E. (1989). Pre-biotic organic matter from comets and asteroids. Nature, 342, 255–7.CrossRefGoogle ScholarPubMed
Bada, J. L., Bigham, C. and Miller, S. L. (1994). Impact melting of frozen oceans on the early Earth: implications for the origin of life. Proceedings of the National Academy of Sciences, USA, 91, 1248–50.CrossRefGoogle ScholarPubMed
Ball, P. (2001). Life's Matrix. Berkeley, CA: University of California Press.Google ScholarPubMed
Beaudry, A. A. and Joyce, G. F. (1992). Directed evolution of an RNA enzyme. Science, 257, 635–41.CrossRefGoogle ScholarPubMed
Brack, A. and Orgel, L. E. (1975). Beta structures of alternating polypeptides and their possible prebiotic significance. Nature, 256, 383–7.CrossRefGoogle ScholarPubMed
Brack, A. and Spach, G. (1981). Enantiomer enrichment in early peptides. Origins of Lifeand the Evolution of Biospheres, 11, 135–42.CrossRefGoogle ScholarPubMed
Chakrabarti, A. C. and Deamer, D. W. (1994). Permeation of membranes by the neutral form of amino acids and peptides: relevance to the origin of peptide translocation. Journal of Molecular Evoution, 39, 1–5.Google ScholarPubMed
Chyba, C. and Sagan, C. (1992). Endogenous production, exogenous delivery and impact-shock synthesis of organic molecules: an inventory for the origins of life. Nature, 355, 125–32.CrossRefGoogle ScholarPubMed
Ehrenfreund, P., Glavin, D. P., Botta, O.et al. (2001). Extraterrestrial amino acids in Orgueil and Ivuna: tracing the parent body of CI type carbonaceous chondrites. Proceedings of the National Academy of Sciences, USA, 98, 2138–42.CrossRefGoogle ScholarPubMed
Eisenberg, D. S. and Kauzmann, W. (1985). The Structure and Properties of Water, 2nd edn. Oxford: Oxford University Press.Google Scholar
Fox, S. W. and Harada, K. (1958). Thermal copolymerization of amino acids to a product resembling protein. Science, 128, 1214.CrossRefGoogle ScholarPubMed
Goto, T., Futamura, Y., Yamaguchi, Y. et al. (2005). Condensation reactions of amino acids under hydrothermal conditions with adiabatic expansion cooling. Journal of Chemical Engineering of Japan, 38, 4: 295–9.
Hargreaves, W. R., Mulvihill, S. J. and Deamer, D. W. (1977). Synthesis of phospholipids and membranes in prebiotic conditions. Nature, 266, 78–80.CrossRefGoogle ScholarPubMed
Henderson, L. J. (1913). The Fitness of the Environment: An Inquiry into the Biological Significance of the Properties of Matter. New York, NY: Macmillan. Repr. (1958) Boston, MA: Beacon Press; (1970) Gloucester, MA: Peter Smith.Google Scholar
Henderson, L. J. (1917) The Order of Nature: An Essay. Cambridge, MA: Harvard University Press.CrossRefGoogle Scholar
Hwang, W., Marini, D, Kamm, R. et al. (2003). Supramolecular structure of helical ribbons self-assembled from a beta-sheet peptide. Journal of Chemical Physics, 118, 389–97.CrossRefGoogle Scholar
Kvenvolden, K., Lawless, J., Pering, K.et al. (1970). Evidence for extraterrestrial amino-acids and hydrocarbons in the Murchison meteorite. Nature, 228, 923–6.CrossRefGoogle ScholarPubMed
Marini, D., Hwang, W., Lauffenburger, D. A.et al. (2002). Left-handed helical ribbon intermediates in the self-assembly of a beta-sheet peptide. NanoLetters, 2, 295–9.CrossRefGoogle Scholar
Miller, S. L. (1953). A production of amino acids under possible primitive earth conditions. Science, 117, 528–9.CrossRefGoogle ScholarPubMed
Miller, S. and Urey, H. C. (1959). Organic compound synthesis on the primitive earth. Science, 130, 245–51.CrossRefGoogle ScholarPubMed
Morowitz, H. J. (1992) Beginning of Cellular Life. New Haven, CT: Yale University Press.Google Scholar
Nagai, A., Nagai, Y., Qu, H.et al. (2007). Dynamic behaviors of lipid-like self-assembling peptide A6D and A6K nanotubes. Journal of Nanoscience and Nanotechnology, 7, 2246–52.CrossRefGoogle ScholarPubMed
Oro, J. and Guidry, C. L. (1961). Direct synthesis of polypeptides. I. Polycondensation of glycine in aqueous ammonia. Archives of Biochemistry and Biophysics, 93, 166–71.CrossRefGoogle ScholarPubMed
Oro, J., and Kamat, S. S. (1961). Amino-acid synthesis from hydrogen cyanide under possible primitive earth conditions. Nature, 190, 442–3.CrossRefGoogle ScholarPubMed
Santoso, S., Hwang, W., Hartman, H.et al. (2002a). Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles. NanoLetters, 2, 687–1.CrossRefGoogle Scholar
Santoso, S., Vauthey, S. and Zhang, S. (2002b). Structures, functions, and applications of amphiphilic peptides. Current Opinion in Colloid and Interface Science, 7, 262–6.CrossRefGoogle Scholar
Vauthey, S.Santoso, S., Gong, H.et al. (2002). Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proceedings of the National Academy of Sciences, USA, 99, 5355–60.CrossRefGoogle ScholarPubMed
Vauthey, Maltzahn G., Santoso, S., S.et al. (2003). Positively charged surfactant-like peptides self-assemble into nanostructures. Langmuir, 19, 4332–7.Google Scholar
White, D. H., Kennedy, R. M. and Macklin, J. (1984). Acyl silicates and acyl aluminates as activated intermediates in peptide formation on clays. Origins of Life and Evolution of Biosphers, 14, 273–8.CrossRefGoogle ScholarPubMed
Wick, R, Angelova, M. I., Walde, P.et al. (1996). Microinjection into giant vesicles and light microscopy investigation of enzyme-mediated vesicle transformations. Chemical Biology, 3, 105.CrossRefGoogle ScholarPubMed
Wilson, C. and Szostak, J. W. (1995). In vitro evolution of a self-alkylating ribozyme. Nature, 374, 777–82.CrossRefGoogle ScholarPubMed
Wong, J. T.-F. and Bronskill, P. M. (1979). Inadequacy of prebiotic synthesis as origin of proteinous amino acids. Journal of Molecular Evolution, 13, 115–25.CrossRefGoogle ScholarPubMed
Yanagawa, H., Ogawa, Y., Kojima, K.et al. (1988). Construction of protocellular structures under simulated primitive earth conditions. Origin of Life and Evolution of Biospheres, 18, 179–207.CrossRefGoogle ScholarPubMed
Yang, S. and Zhang, S. (2006) Self-assembling behavior of designer lipid-like peptides. Supramolecular Chemistry, 18, 389–96.CrossRefGoogle Scholar
Zhang, S. (2003). Fabrication of novel materials through molecular self-assembly. Nature Biotechnology, 21, 1171–8.CrossRefGoogle ScholarPubMed
Zhang, S. and Egli, M. (1994). A hypothesis: reciprocal information transfer between oligoribonucleotides and oligopeptides in prebiotic molecular evolution. Origins of Life and Evolution of Biospheres, 24, 495–505.CrossRefGoogle ScholarPubMed
Zhang, S. and Egli, M. (1995). A proposed complementary pairing mode between single-stranded nucleic acids and b-stranded peptides: a possible pathway for generating complex biological molecules. Complexity, 1, 49–56.CrossRefGoogle Scholar
Zhang, S., Holmes, T., Lockshin, C.et al. (1993). Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proceedings of the National Academy of Sciences, USA, 90, 3334–8.CrossRefGoogle Scholar
Zhang, S., Marini, D., Hwang, W.et al. (2002). Design nanobiological materials through self-assembly of peptide and proteins. Current Opinion in Chemical Biology, 6, 865–71.CrossRefGoogle Scholar
Zhao, X. and Zhang, S. (2004). Design molecular biological materials using peptide motifs. Trends in Biotechnology, 22, 470–6.CrossRefGoogle Scholar

Save book to Kindle

To save this book to your Kindle, first ensure [email protected] is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×