NOVELTY - A self-complementary beta -strand peptide (P1) comprising alternating hydrogen bonding proton donor and acceptor amino acid segments having a length of four to forty amino acids is new. The hydrogen bonding proton donor/acceptor amino acid segment consists of at least one amino acid; the beta -strand peptide comprises at least one proton donor segment and at least one proton acceptor segment. The peptide is not comprised of alternating hydrophobic and hydrophilic amino acid segments. The self-complementary beta -strand peptides assemble into the nanostructure.    USE - For manufacture of beta -strand peptide-based nanostructure i.e. nanofibril, nanowire, nanosurface and nanosphere; for forming a biofuel cell; for identification of inhibitors of protein aggregation disease; for altering the wettability and biocompatibility property of a surface; for detecting a biomolecule of interest particularly proteins, nucleic acids, carbohydrates, viruses and glucose; for manufacturing pharmaceutical composition; for delivery of a therapeutic agent particularly hydrophobic agent, hydrophilic and oligonucleotide (claimed) and gene; as drug delivery vehicles; for solubilizing hydrophobic drugs such as ellipticine, an anti-cancer drug in its protonated or neutral form; in biomolecule sensory; for generating models to study protein conformation diseases, such as Alzheimer's and prion disorders; in proteomics and bioinformatics applications; for modification of array surfaces where the functional residues of the peptide can immobilize DNA and protein molecules on the array; for coating applications including coating for the prevention of biofouling; in biocompatible surface coating and coating for functionalized chromatographic columns; for modification of surface coatings.    ADVANTAGE - The solubilized drugs formed by peptides are more protected and stable inside the peptide vehicles i.e. approximately 16-fold dilution in water. The peptides seeded onto a hydrophobic surface can assemble into different nanostructures, thus can be shaped into specific nanostructures depending on the nature of the surface on which they are seeded, and peptide-modification of a surface can result in changes to the surface wettability, therefore peptide-modified surfaces are effective for biomolecule sensing applications. Peptides bind to biomolecules such as enzymes for use in sensing enzymatic substrates, and immobilize the biomolecules on the surface. The peptides can be immobilized on electrodes where they are bound to biosensory molecules such as enzymes, and the enzymatic substrates can be added to drive the catalytic reaction. Such biofuel cells have strong storage and operational stabilities. The peptides are used in proteomics and bioinformatics applications, where the molecular dynamics simulations can be applied to screen all potential pairs of amino acids that can complementarily interact with each other, and this information is useful in peptide library development, manufacturing protein/peptide and DNA arrays for high throughput screening and validation studies. Peptides are useful to modify array surfaces where the functional residues of the peptide can immobilize DNA and protein molecules on the array. The peptides in coating applications provide prevention of biofouling and a biocompatible environment for protein/enzyme immobilization.    DETAILED DESCRIPTION - INDEPENDENT CLAIMS are included for the following:    (1) new self-complementary beta -strand peptide (P2) comprising at least one hydrogen bonding amino acid pair, at least one ionic-complementary amino acid pair, at least one hydrophobic amino acid pair, and having a length of four to forty amino acids;    (2) preparation of the peptide;    (3) a pharmaceutical composition comprising the peptide (P1) and (P2) and a therapeutic agent;    (4) a kit for delivering a material to a patient comprising the pharmaceutical composition; and at least one of an electrolyte, a buffer, a delivery device, and a vessel for mixing the composition with at least one other agents; and instructions for preparing the composition for use, instructions for mixing the composition with other agents, and instructions for administering the composition;    (5) method for detecting desired biomolecule involving forming a nanostructure from the peptide upon self assembly; adsorbing the peptide to an electrode surface, allowing electron transfer and immobilization of biocatalysts; coupling a reporter molecule capable of providing a measurable signal to the peptide-coated surface of the nanostructure; and providing the biomolecule;    (6) use of the peptide for forming a biofuel cell;    (7) a self-assembled nanostructure consisting of aggregated units of the peptide of formula (A1xB1yC1z)w (I), (A1xB1yC1z)wA1x (II) or (A2w'B2x'A2y'C1z')nA2aB2b (V).    A1, B1 and C1=hydrogen bonding amino acid selected from proton donors and proton acceptors;    x and y=1-10;    z=0-10;    w=1-20;    A2, B2 and C2=amino acid selected from a hydrophobic amino acid, a charged amino acid, or a hydrogen bonding amino acid;    w', x', y'and z'=1-5;    a and b=0-2;and    n=1-10.